EzCatDB: D00101

DB codeD00101
RLCP classification6.30.97700.5320
8.211.591510.5526
6.20.85200.5520
6.10.82600.5900
8.211.591510.5527
6.40.521000.5530
CATH domainDomain 13.90.1150.10
Domain 23.40.640.10Catalytic domain
E.C.2.6.1.1
CSA1aam,2aat

CATH domainRelated DB codes (homologues)
3.40.640.10D00085,D00092,D00102,D00103,D00104,D00107,D00108,D00109,D00255,D00257,D00258,D00265,D00269,D00515,M00031,D00279
3.90.1150.10D00085,D00092,D00102,D00103,D00104,D00107,D00108,D00109,D00255,D00257,D00258,D00265,D00269,D00515,M00031,D00279

Enzyme Name
Swiss-protKEGG

P00503P00504P00508P00509P23542Q56232
Protein nameAspartate aminotransferase, cytoplasmicAspartate aminotransferase, cytoplasmicAspartate aminotransferase, mitochondrialAspartate aminotransferaseAspartate aminotransferase, cytoplasmicAspartate aminotransferaseaspartate transaminase
glutamic-oxaloacetic transaminase
glutamic-aspartic transaminase
transaminase A
AAT
AspT
2-oxoglutarate-glutamate aminotransferase
aspartate alpha-ketoglutarate transaminase
aspartate aminotransferase
aspartate-2-oxoglutarate transaminase
aspartic acid aminotransferase
aspartic aminotransferase
aspartyl aminotransferase
AST
glutamate-oxalacetate aminotransferase
glutamate-oxalate transaminase
glutamic-aspartic aminotransferase
glutamic-oxalacetic transaminase
glutamic oxalic transaminase
GOT (enzyme)
L-aspartate transaminase
L-aspartate-alpha-ketoglutarate transaminase
L-aspartate-2-ketoglutarate aminotransferase
L-aspartate-2-oxoglutarate aminotransferase
L-aspartate-2-oxoglutarate-transaminase
L-aspartic aminotransferase
oxaloacetate-aspartate aminotransferase
oxaloacetate transferase
aspartate:2-oxoglutarate aminotransferase
glutamate oxaloacetate transaminase
SynonymsEC 2.6.1.1
Transaminase A
Glutamate oxaloacetate transaminase 1
EC 2.6.1.1
Transaminase A
Glutamate oxaloacetate transaminase 1
EC 2.6.1.1
Transaminase A
Glutamate oxaloacetate transaminase 2
AspAT
EC 2.6.1.1
Transaminase A
EC 2.6.1.1
Transaminase A
AspAT
EC 2.6.1.1
Transaminase A

KEGG pathways
MAP codePathways
MAP00251Glutamate metabolism
MAP00252Alanine and aspartate metabolism
MAP00272Cysteine metabolism
MAP00330Arginine and proline metabolism
MAP00350Tyrosine metabolism
MAP00360Phenylalanine metabolism
MAP00400Phenylalanine, tyrosine and tryptophan biosynthesis
MAP00401Novobiocin biosynthesis
MAP00710Carbon fixation in photosynthetic organisms
MAP00950Alkaloid biosynthesis I

Swiss-prot:Accession NumberP00503P00504P00508P00509P23542Q56232
Entry nameAATC_PIGAATC_CHICKAATM_CHICKAAT_ECOLIAATC_YEASTAAT_THET8
ActivityL-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.
SubunitHomodimer.Homodimer.Homodimer.Homodimer.Homodimer.Homodimer.
Subcellular locationCytoplasm.Cytoplasm.Mitochondrion matrix.Cytoplasm.Cytoplasm. Peroxisome. Note=Targeted to peroxisomes in cells grown in oleate.Cytoplasm (By similarity).
CofactorPyridoxal phosphate.Pyridoxal phosphate.Pyridoxal phosphate.Pyridoxal phosphate.Pyridoxal phosphate.Pyridoxal phosphate.


CofactorsSubstratesProductsintermediates
KEGG-idC00018C00026C00049C00025C00036I00004I00034I00005
C00647I00006I00033I00007
CompoundPyridoxal phosphate2-OxoglutarateL-AspartateL-GlutamateOxaloacetateExternal aldimine intermediate (initial stage:PLP-Asp)Quinonoid intermediate-1 (PLP-Asp)Ketimine intermediate-1 (PLP-Asp)Tetrahedral intermediate from ketimine to PMP Pyridoxamine phosphate (PMP)Ketimine intermediate-2 (PLP-Glu)Quinonoid intermediate-2 (PLP-Glu)External aldimine intermediate (final stage:PLP-Glu)
Typearomatic ring (with nitrogen atoms),phosphate group/phosphate ioncarbohydrate,carboxyl groupamino acids,carboxyl groupamino acids,carboxyl groupcarbohydrate,carboxyl group







1aamA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1aawA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1aheA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1aheB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ahfA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ahfB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ahgA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ahgB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ahxA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ahxB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ahyA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ahyB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1aiaA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1aiaB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1aibA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1aibB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1aicA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1aicB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ajrA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ajrB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ajsA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ajsB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1akaA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1akaB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1akbA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1akcA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1amaA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1amqA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1amrA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1amsA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1argA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1argB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1arhA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1arhB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ariA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ariB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1arsA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1artA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1asaA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1asbA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ascA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1asdA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1aseA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1asfA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1asgA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1aslA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1aslB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1asmA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1asmB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1asnA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1asnB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1b4xA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1bjwA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1bjwB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1bkgA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1bkgB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1bkgC01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1bkgD01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1bqaA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1bqaB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1bqdA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1bqdB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1c9cA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cq6A01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cq7A01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cq8A01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1czcA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1czeA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1g4vA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1g4xA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1g7wA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1g7xA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ivrA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1mapA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1maqA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1oxoA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1oxoB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1oxpA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qirA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qisA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qitA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1spaA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1tarA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1tarB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1tasA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1tasB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1tatA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1tatB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1yaaA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1yaaB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1yaaC01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1yaaD01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1yooA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2aatA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2cstA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2cstB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3aatA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
5eaaA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
7aatA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
7aatB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
8aatA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
8aatB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
9aatA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
9aatB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1aamA02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1aawA02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1aheA02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1aheB02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ahfA02Bound:PLPUnboundAnalogue:IOPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ahfB02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ahgA02Bound:PLPUnboundUnboundUnboundUnboundIntermediate-analogue:PLP-TYRUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:PLP-TYR
1ahgB02Bound:PLPUnboundUnboundUnboundUnboundIntermediate-analogue:PLP-TYRUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:PLP-TYR
1ahxA02Bound:PLPAnalogue:HCIUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ahxB02Bound:PLPAnalogue:HCIUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ahyA02Bound:PLPUnboundAnalogue:MAEUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ahyB02Bound:PLPUnboundAnalogue:MAEUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1aiaA02Analogue:PMPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-bound:PMPUnboundUnboundUnbound
1aiaB02Analogue:PMPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-bound:PMPUnboundUnboundUnbound
1aibA02Analogue:PMPBound:AKGUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-bound:PMPUnboundUnboundUnbound
1aibB02Analogue:PMPBound:AKGUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-bound:PMPUnboundUnboundUnbound
1aicA02Analogue:PMPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-bound:PMPUnboundUnboundUnbound
1aicB02Analogue:PMPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-bound:PMPUnboundUnboundUnbound
1ajrA02Bound:LLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ajrB02Bound:LLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ajsA02Analogue:PLAUnboundUnboundUnboundUnboundIntermediate-analogue:PLAUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ajsB02Bound:LLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1akaA02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1akaB02UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1akbA02Analogue:PPDUnboundUnboundUnboundUnboundIntermediate-Bound:PPDUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1akcA02Analogue:PPEUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-Bound:PPE
1amaA02Analogue:PLAUnboundUnboundUnboundUnboundIntermediate-analogue:PLAUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1amqA02Analogue:PMPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-bound:PMPUnboundUnboundUnbound
1amrA02Analogue:PMPUnboundAnalogue:MAEUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-bound:PMPUnboundUnboundUnbound
1amsA02Analogue:PMPAnalogue:GUAUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-bound:PMPUnboundUnboundUnbound
1argA02Analogue:PPDUnboundUnboundUnboundUnboundIntermediate-Bound:PPDUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1argB02Analogue:PPDUnboundUnboundUnboundUnboundIntermediate-Bound:PPDUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1arhA02Analogue:PPDUnboundUnboundUnboundUnboundIntermediate-Bound:PPDUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1arhB02Analogue:PPDUnboundUnboundUnboundUnboundIntermediate-Bound:PPDUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ariA02Bound:PLPUnboundAnalogue:MAEUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ariB02Bound:PLPUnboundAnalogue:MAEUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1arsA02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1artA02Bound:PLPUnboundUnboundUnboundUnboundIntermediate-analogue:PLP-ASP-CH3UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1asaA02Bound:PLPUnboundAnalogue:MAEUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1asbA02Bound:PLPUnboundAnalogue:MAEUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ascA02Analogue:NPLUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:NPLUnboundUnboundUnbound
1asdA02Analogue:MPLUnboundAnalogue:MAEUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1aseA02Analogue:NOPUnboundAnalogue:MAEUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1asfA02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1asgA02Bound:PLPUnboundAnalogue:MAEUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1aslA02Analogue:PLAUnboundUnboundUnboundUnboundIntermediate-analogue:PLAUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1aslB02Analogue:PLAUnboundUnboundUnboundUnboundIntermediate-analogue:PLAUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1asmA02Bound:PLPUnboundAnalogue:MAEUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1asmB02Bound:PLPUnboundAnalogue:MAEUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1asnA02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1asnB02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1b4xA02Bound:PLPUnboundAnalogue:MAEUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1bjwA02Bound:LLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1bjwB02Bound:LLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1bkgA02Analogue:PMPUnboundAnalogue:MAEUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-bound:PMPUnboundUnboundUnbound
1bkgB02Analogue:PMPUnboundAnalogue:MAEUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-bound:PMPUnboundUnboundUnbound
1bkgC02Analogue:PMPUnboundAnalogue:MAEUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-bound:PMPUnboundUnboundUnbound
1bkgD02Analogue:PMPUnboundAnalogue:MAEUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-bound:PMPUnboundUnboundUnbound
1bqaA02Bound:LLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1bqaB02Bound:LLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1bqdA02Bound:LLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1bqdB02Bound:LLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1c9cA02Analogue:PP3UnboundUnboundUnboundUnboundIntermediate-analogue:PP3UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cq6A02Analogue:PY4UnboundUnboundUnboundUnboundIntermediate-analogue:PY4UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cq7A02Analogue:PY5UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:PY5
1cq8A02Analogue:PY6UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:PY6
1czcA02Bound:PLPAnalogue:GUAUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1czeA02Bound:PLPUnboundAnalogue:SINUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1g4vA02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1g4xA02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1g7wA02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1g7xA02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ivrA02Analogue:CBAUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:CBAUnboundUnboundUnboundUnbound
1mapA02Analogue:KETUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-bound:KETUnboundUnboundUnboundUnboundUnbound
1maqA02Analogue:PGUUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-bound:PGUUnboundUnbound
1oxoA02Analogue:IK2UnboundUnboundUnboundUnboundIntermediate-analogue:IK2UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1oxoB02Analogue:IK2UnboundUnboundUnboundUnboundIntermediate-analogue:IK2UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1oxpA02Analogue:IK2UnboundUnboundUnboundUnboundIntermediate-analogue:IK2UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qirA02Bound:PLPUnboundAnalogue:MAEUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qisA02Bound:PLPUnboundAnalogue:MAEUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qitA02Bound:PLPUnboundAnalogue:MAEUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1spaA02Analogue:NPLUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:NPLUnboundUnboundUnbound
1tarA02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1tarB02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1tasA02Analogue:PLAUnboundUnboundUnboundUnboundIntermediate-analogue:PLAUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1tasB02Analogue:PLAUnboundUnboundUnboundUnboundIntermediate-analogue:PLAUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1tatA02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1tatB02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1yaaA02Bound:PLPUnboundAnalogue:MAEUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1yaaB02Bound:PLPUnboundAnalogue:MAEUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1yaaC02Bound:PLPUnboundAnalogue:MAEUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1yaaD02Bound:PLPUnboundAnalogue:MAEUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1yooA02Bound:PLPUnboundAnalogue:IVAUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2aatA02Analogue:PMPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-bound:PMPUnboundUnboundUnbound
2cstA02Bound:PLPUnboundAnalogue:MAEUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2cstB02Bound:PLPUnboundAnalogue:MAEUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3aatA02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
5eaaA02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
7aatA02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
7aatB02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
8aatA02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
8aatB02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
9aatA02Analogue:PMPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-bound:PMPUnboundUnboundUnbound
9aatB02Analogue:PMPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-bound:PMPUnboundUnboundUnbound

Active-site residues
pdbCatalytic residuesCofactor-binding residuesModified residuescomment
1aamA01



1aawA01



1aheA01


mutant V39L, K41Y, T47I
1aheB01


mutant V39L, K41Y, T47I
1ahfA01


mutant V39L, K41Y, T47I
1ahfB01


mutant V39L, K41Y, T47I
1ahgA01


mutant V39L, K41Y, T47I
1ahgB01


mutant V39L, K41Y, T47I
1ahxA01


mutant V39L, K41Y, T47I
1ahxB01


mutant V39L, K41Y, T47I
1ahyA01


mutant V39L, K41Y, T47I
1ahyB01


mutant V39L, K41Y, T47I
1aiaA01



1aiaB01



1aibA01



1aibB01



1aicA01



1aicB01



1ajrA01



1ajrB01



1ajsA01



1ajsB01



1akaA01



1akaB01



1akbA01



1akcA01



1amaA01



1amqA01



1amrA01



1amsA01



1argA01



1argB01



1arhA01



1arhB01



1ariA01



1ariB01



1arsA01



1artA01



1asaA01



1asbA01



1ascA01



1asdA01



1aseA01



1asfA01



1asgA01



1aslA01



1aslB01



1asmA01



1asmB01



1asnA01



1asnB01



1b4xA01



1bjwA01



1bjwB01



1bkgA01



1bkgB01



1bkgC01



1bkgD01



1bqaA01



1bqaB01



1bqdA01



1bqdB01



1c9cA01



1cq6A01



1cq7A01



1cq8A01



1czcA01



1czeA01



1g4vA01



1g4xA01



1g7wA01



1g7xA01



1ivrA01



1mapA01



1maqA01



1oxoA01



1oxoB01



1oxpA01



1qirA01



1qisA01



1qitA01



1spaA01



1tarA01



1tarB01



1tasA01



1tasB01



1tatA01



1tatB01



1yaaA01



1yaaB01



1yaaC01



1yaaD01



1yooA01


mutant A11T, F24L, N34D, I37M, K41N, I353T, S361F, S363G, V387L, M397L
2aatA01



2cstA01



2cstB01



3aatA01



5eaaA01



7aatA01



7aatB01



8aatA01



8aatB01



9aatA01



9aatB01



1aamA02TYR 77;ASP 223;TYR 226;LYS 258
LYS 258(PLP binding)

mutant R292D
1aawA02TYR 77;ASP 223;TYR 226;LYS 258
LYS 258(PLP binding)


1aheA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)

mutant N69L, T109S, N297S
1aheB02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)

mutant N69L, T109S, N297S
1ahfA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)

mutant N69L, T109S, N297S
1ahfB02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)

mutant N69L, T109S, N297S
1ahgA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)

mutant N69L, T109S, N297S
1ahgB02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)

mutant N69L, T109S, N297S
1ahxA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)

mutant N69L, T109S, N297S
1ahxB02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)

mutant N69L, T109S, N297S
1ahyA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)

mutant N69L, T109S, N297S
1ahyB02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)

mutant N69L, T109S, N297S
1aiaA02TYR 70;ASP 222;TYR 225;       
                    

mutant K258H
1aiaB02TYR 70;ASP 222;TYR 225;       
                    

mutant K258H
1aibA02TYR 70;ASP 222;TYR 225;       
                    

mutant K258H
1aibB02TYR 70;ASP 222;TYR 225;       
                    

mutant K258H
1aicA02TYR 70;ASP 222;TYR 225;       
                    

mutant K258H
1aicB02TYR 70;ASP 222;TYR 225;       
                    

mutant K258H
1ajrA02TYR 70;ASP 222;TYR 225;       
                    
LLP 258(PLP-binding Lys)

1ajrB02TYR 70;ASP 222;TYR 225;       
                    
LLP 258(PLP-binding Lys)

1ajsA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1ajsB02TYR 70;ASP 222;TYR 225;       
                    
LLP 258(PLP-binding Lys)

1akaA02TYR 70;ASP 222;TYR 225;       
                    

mutant K258H
1akaB02TYR 70;ASP 222;TYR 225;       
                    

mutant K258H
1akbA02TYR 70;ASP 222;TYR 225;       
                    

mutant K258H
1akcA02TYR 70;ASP 222;TYR 225;       
                    

mutant K258H
1amaA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1amqA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1amrA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1amsA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1argA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1argB02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1arhA02TYR 70;ASP 222;       ;LYS 258
LYS 258(PLP binding)

mutant Y225R, R386A
1arhB02TYR 70;ASP 222;       ;LYS 258
LYS 258(PLP binding)

mutant Y225R, R386A
1ariA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)

mutant W140H
1ariB02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)

mutant W140H
1arsA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1artA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1asaA02TYR 77;ASP 223;TYR 226;LYS 258
LYS 258(PLP binding)


1asbA02TYR 77;       ;TYR 226;LYS 258
LYS 258(PLP binding)

mutant D223A
1ascA02TYR 77;       ;TYR 226;LYS 258
LYS 258(PLP binding)

mutant D223A
1asdA02TYR 77;ASP 223;TYR 226;LYS 258
LYS 258(PLP binding)


1aseA02TYR 77;ASP 223;TYR 226;LYS 258
LYS 258(PLP binding)


1asfA02TYR 77;ASP 223;       ;LYS 258
LYS 258(PLP binding)

mutant Y226F
1asgA02TYR 77;ASP 223;       ;LYS 258
LYS 258(PLP binding)

mutant Y226F
1aslA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1aslB02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1asmA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1asmB02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1asnA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1asnB02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1b4xA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)

mutant C191S
1bjwA02TYR 64;ASP 203;TYR 206;       
                    
LLP 234(PLP-binding Lys)

1bjwB02TYR 64;ASP 203;TYR 206;       
                    
LLP 234(PLP-binding Lys)

1bkgA02TYR 64;ASP 203;TYR 206;LYS 234
LYS 234(PLP binding)


1bkgB02TYR 64;ASP 203;TYR 206;LYS 234
LYS 234(PLP binding)


1bkgC02TYR 64;ASP 203;TYR 206;LYS 234
LYS 234(PLP binding)


1bkgD02TYR 64;ASP 203;TYR 206;LYS 234
LYS 234(PLP binding)


1bqaA02TYR 70;ASP 222;TYR 225;       
                    
LLP 258(PLP-binding Lys)
mutant P195A
1bqaB02TYR 70;ASP 222;TYR 225;       
                    
LLP 258(PLP-binding Lys)
mutant P195A
1bqdA02TYR 70;ASP 222;TYR 225;       
                    
LLP 258(PLP-binding Lys)
mutant P138A, P195A
1bqdB02TYR 70;ASP 222;TYR 225;       
                    
LLP 258(PLP-binding Lys)
mutant P138A, P195A
1c9cA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1cq6A02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1cq7A02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1cq8A02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1czcA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1czeA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1g4vA02TYR 70;ASP 222;       ;LYS 258
LYS 258(PLP binding)

mutant N194A, Y225F
1g4xA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)

mutant N194A, Y292L
1g7wA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)

mutant N194A, R386L
1g7xA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)

mutant N194A, R292L, R386L
1ivrA02TYR 67;ASP 214;TYR 217;LYS 250
LYS 250(PLP binding)


1mapA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1maqA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1oxoA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1oxoB02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1oxpA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1qirA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)

mutant C191Y
1qisA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)

mutant C191F
1qitA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)

mutant C191W
1spaA02TYR 70;       ;TYR 225;LYS 258
LYS 258(PLP binding)

mutant D222A
1tarA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1tarB02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1tasA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1tasB02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1tatA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1tatB02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1yaaA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1yaaB02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1yaaC02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1yaaD02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


1yooA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)

mutant K126R, S139G, N142T, A269T, A293V, N297S, S311G
2aatA02TYR 77;ASP 223;TYR 226;       
                    

mutant K258A
2cstA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


2cstB02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


3aatA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)

mutant R386F
5eaaA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)

mutant C191S
7aatA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


7aatB02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


8aatA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


8aatB02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


9aatA02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)


9aatB02TYR 70;ASP 222;TYR 225;LYS 258
LYS 258(PLP binding)



References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]Scheme I, p.8648-8649
[5]p.8163-8166
[7]p.180-181
[9]p.1984
[11]

[12]Scheme 1
[13]Scheme 2, p.574-576
[15]Fig.1
[17]Fig.1, p.5883-5886
[18]Fig.1, p.510-514
[20]Scheme 1, Scheme 2, p.115-116
[21]Scheme I, p.13460-13461
[22]Scheme 1, p.482-483
[24]

[26]Scheme 2, p.1010-1011
[27]Scheme 2, p.104-105
[30]p.409-411
[32]Scheme 1
[33]Scheme 1, Chart 1, p.9419-9422
[34]Scheme 1, p.413-414
[35]Scheme 1, p.688-689
[39]Fig.1, p.15265-15267
[46]Scheme 1, p.15080-15085
[53]Scheme 1
[59]Scheme 1, Chart 1, p.356
[61]Scheme I, Fig.5, p.9487-9488

references
[1]
CommentsACTIVE SITE
Medline ID69285398
PubMed ID5809231
JournalBiochemistry
Year1969
Volume8
Pages3412-7
AuthorsMorino Y, Watanabe T
TitlePrimary structure of pyridoxal phosphate binding site in the mitochondrial and extramitochondrial aspartate aminotransferases from pig heart muscle. Chymotryptic peptides.
Related Swiss-protP00503
[2]
CommentsACTIVE SITE
Medline ID73044407
PubMed ID4634443
JournalFEBS Lett
Year1972
Volume23
Pages262-4
AuthorsPolyanovsky OL, Demidkina TV
TitleThe position of an essential tyrosine residue in the polypeptide chain of aspartate transaminase.
Related Swiss-protP00503
[3]
PubMed ID7410385
JournalJ Biol Chem
Year1980
Volume255
Pages8645-9
AuthorsZito SW, Martinez-Carrion M
TitleStereospecificity of sodium borohydride reduction of Schiff bases at the active site of aspartate aminotransferase.
[4]
CommentsX-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS)
Medline ID80143195
PubMed ID7360247
JournalNature
Year1980
Volume284
Pages189-90
AuthorsBorisov VV, Borisova SN, Sosfenov NI, Vainshtein BK
TitleElectron density map of chicken heart cytosol aspartate transaminase at 3.5 A resolution.
Related Swiss-protP00504
[5]
CommentsX-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS)
Medline ID82165126
PubMed ID7067826
JournalFEBS Lett
Year1982
Volume138
Pages113-6
AuthorsHarutyunyan EG, Malashkevich VN, Tersyan SS, Kochkina VM, Torchinsky YuM, Braunstein AE
TitleThree-dimensional structure at 3.2 A resolution of the complex of cytosolic aspartate aminotransferase from chicken heart with 2-oxoglutarate.
Related Swiss-protP00504
[6]
CommentsX-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT ALA-246
Medline ID90105323
PubMed ID2513875
JournalBiochemistry
Year1989
Volume28
Pages8161-7
AuthorsSmith DL, Almo SC, Toney MD, Ringe D
Title2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli.
Related PDB2aat
Related Swiss-protP00509
[7]
PubMed ID2121725
JournalJ Biochem (Tokyo)
Year1990
Volume108
Pages175-84
AuthorsKamitori S, Okamoto A, Hirotsu K, Higuchi T, Kuramitsu S, Kagamiyama H, Matsuura Y, Katsube Y
TitleThree-dimensional structures of aspartate aminotransferase from Escherichia coli and its mutant enzyme at 2.5 A resolution.
[8]
PubMed ID2231709
JournalJ Mol Biol
Year1990
Volume215
Pages341-4
AuthorsIzard T, Fol B, Pauptit RA, Jansonius JN
TitleTrigonal crystals of porcine mitochondrial aspartate aminotransferase.
[9]
CommentsX-RAY CRYSTALLOGRAPHY, AND MUTAGENESIS OF ARG-374
Medline ID91129283
PubMed ID1993208
JournalBiochemistry
Year1991
Volume30
Pages1980-5
AuthorsDanishefsky AT, Onnufer JJ, Petsko GA, Ringe D
TitleActivity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase.
Related PDB3aat
Related Swiss-protP00509
[10]
PubMed ID2015218
JournalBiochemistry
Year1991
Volume30
Pages3612-20
AuthorsHerold M, Leistler B, Hage A, Luger K, Kirschner K
TitleAutonomous folding and coenzyme binding of the excised pyridoxal 5'-phosphate binding domain of aspartate aminotransferase from Escherichia coli.
[11]
CommentsMUTAGENESIS OF TYR-65
Medline ID91329346
PubMed ID1868057
JournalBiochemistry
Year1991
Volume30
Pages7796-801
AuthorsInoue K, Kuramitsu S, Okamoto A, Hirotsu K, Higuchi T, Kagamiyama H
TitleSite-directed mutagenesis of Escherichia coli aspartate aminotransferase: role of Tyr70 in the catalytic processes.
Related Swiss-protP00509
[12]
PubMed ID2007402
JournalEur J Biochem
Year1991
Volume196
Pages329-41
AuthorsPicot D, Sandmeier E, Thaller C, Vincent MG, Christen P, Jansonius JN
TitleThe open/closed conformational equilibrium of aspartate aminotransferase. Studies in the crystalline state and with a fluorescent probe in solution.
[13]
PubMed ID1869510
JournalJ Biochem (Tokyo)
Year1991
Volume109
Pages570-6
AuthorsInoue K, Kuramitsu S, Okamoto A, Hirotsu K, Higuchi T, Morino Y, Kagamiyama H
TitleTyr225 in aspartate aminotransferase: contribution of the hydrogen bond between Tyr225 and coenzyme to the catalytic reaction.
[14]
PubMed ID1990006
JournalJ Biol Chem
Year1991
Volume266
Pages2567-72
AuthorsSung MH, Tanizawa K, Tanaka H, Kuramitsu S, Kagamiyama H, Hirotsu K, Okamoto A, Higuchi T, Soda K
TitleThermostable aspartate aminotransferase from a thermophilic Bacillus species. Gene cloning, sequence determination, and preliminary x-ray characterization.
[15]
CommentsMUTAGENESIS OF HIS-133
Medline ID91177849
PubMed ID2007566
JournalJ Biol Chem
Year1991
Volume266
Pages6079-85
AuthorsYano T, Kuramitsu S, Tanase S, Morino Y, Hiromi K, Kagamiyama H
TitleThe role of His143 in the catalytic mechanism of Escherichia coli aspartate aminotransferase.
Related Swiss-protP00509
[16]
PubMed ID1920419
JournalJ Mol Biol
Year1991
Volume221
Pages61-3
AuthorsMalashkevich VN, Sinitzina NI
TitleNew crystal form of cytosolic chicken aspartate aminotransferase suitable for high-resolution X-ray analysis.
[17]
CommentsX-ray crystallography
PubMed ID1610831
JournalBiochemistry
Year1992
Volume31
Pages5878-87
AuthorsYano T, Kuramitsu S, Tanase S, Morino Y, Kagamiyama H
TitleRole of Asp222 in the catalytic mechanism of Escherichia coli aspartate aminotransferase: the amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal 5'-phosphate.
Related PDB1spa
[18]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS)
Medline ID92277655
PubMed ID1593633
JournalJ Mol Biol
Year1992
Volume225
Pages495-517
AuthorsMcPhalen CA, Vincent MG, Jansonius JN
TitleX-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase.
Related PDB7aat,8aat,9aat
Related Swiss-protP00508
[19]
CommentsX-ray crystallography
PubMed ID1522585
JournalJ Mol Biol
Year1992
Volume227
Pages197-213
AuthorsMcPhalen CA, Vincent MG, Picot D, Jansonius JN, Lesk AM, Chothia C
TitleDomain closure in mitochondrial aspartate aminotransferase.
Related PDB1ama
[20]
PubMed ID1339023
JournalProtein Sci
Year1992
Volume1
Pages107-19
AuthorsToney MD, Kirsch JF
TitleBronsted analysis of aspartate aminotransferase via exogenous catalysis of reactions of an inactive mutant.
[21]
CommentsX-ray crystallography
PubMed ID7903048
JournalBiochemistry
Year1993
Volume32
Pages13451-62
AuthorsMalashkevich VN, Toney MD, Jansonius JN
TitleCrystal structures of true enzymatic reaction intermediates: aspartate and glutamate ketimines in aspartate aminotransferase.
Related PDB1map,1maq
[22]
PubMed ID8436109
JournalEur J Biochem
Year1993
Volume211
Pages475-84
AuthorsZiak M, Jager J, Malashkevich VN, Gehring H, Jaussi R, Jansonius JN, Christen P
TitleMutant aspartate aminotransferase (K258H) without pyridoxal-5'-phosphate-binding lysine residue. Structural and catalytic properties.
[23]
PubMed ID8227035
JournalJ Biol Chem
Year1993
Volume268
Pages24758-65
AuthorsPan QW, Tanase S, Fukumoto Y, Nagashima F, Rhee S, Rogers PH, Arnone A, Morino Y
TitleFunctional roles of valine 37 and glycine 38 in the mobile loop of porcine cytosolic aspartate aminotransferase.
[24]
PubMed ID8263922
JournalJ Mol Biol
Year1993
Volume234
Pages1218-29
AuthorsYano T, Hinoue Y, Chen VJ, Metzler DE, Miyahara I, Hirotsu K, Kagamiyama H
TitleRole of an active site residue analyzed by combination of mutagenesis and coenzyme analog.
[25]
PubMed ID8112350
JournalEur J Biochem
Year1994
Volume219
Pages993-1000
AuthorsSterk M, Hauser H, Marsh D, Gehring H
TitleProbing conformational states of spin-labeled aspartate aminotransferase by ESR.
[26]
CommentsX-ray crystallography
PubMed ID7896726
JournalJ Biochem (Tokyo)
Year1994
Volume116
Pages1001-12
AuthorsMiyahara I, Hirotsu K, Hayashi H, Kagamiyama H
TitleX-ray crystallographic study of pyridoxamine 5'-phosphate-type aspartate aminotransferases from Escherichia coli in three forms.
Related PDB1amq,1amr,1ams
[27]
CommentsX-ray crystallography
PubMed ID7798192
JournalJ Biochem (Tokyo)
Year1994
Volume116
Pages95-107
AuthorsOkamoto A, Higuchi T, Hirotsu K, Kuramitsu S, Kagamiyama H
TitleX-ray crystallographic study of pyridoxal 5'-phosphate-type aspartate aminotransferases from Escherichia coli in open and closed form.
Related PDB1ars,1art
[28]
CommentsX-ray crystallography
PubMed ID8120903
JournalJ Mol Biol
Year1994
Volume236
Pages963-8
AuthorsHohenester E, Jansonius JN
TitleCrystalline mitochondrial aspartate aminotransferase exists in only two conformations.
Related PDB1tar,1tas,1tat
[29]
CommentsX-ray crystallography
PubMed ID8196059
JournalJ Mol Biol
Year1994
Volume239
Pages285-305
AuthorsJager J, Moser M, Sauder U, Jansonius JN
TitleCrystal structures of Escherichia coli aspartate aminotransferase in two conformations. Comparison of an unliganded open and two liganded closed forms.
Related PDB1asl,1asm,1asn
[30]
CommentsX-ray crystallography
PubMed ID7909946
JournalProtein Eng
Year1994
Volume7
Pages405-12
AuthorsAlmo SC, Smith DL, Danishefsky AT, Ringe D
TitleThe structural basis for the altered substrate specificity of the R292D active site mutant of aspartate aminotransferase from E. coli.
Related PDB1aam,1aaw,1asa,1asb,1asc,1asd,1ase,1asf
[31]
PubMed ID8073030
JournalProtein Eng
Year1994
Volume7
Pages605-12
AuthorsJager J, Pauptit RA, Sauder U, Jansonius JN
TitleThree-dimensional structure of a mutant E. coli aspartate aminotransferase with increased enzymic activity.
[32]
PubMed ID7547975
JournalBiochemistry
Year1995
Volume34
Pages12323-32
AuthorsGloss LM, Kirsch JF
TitleExamining the structural and chemical flexibility of the active site base, Lys-258, of Escherichia coli aspartate aminotransferase by replacement with unnatural amino acids.
[33]
PubMed ID7626611
JournalBiochemistry
Year1995
Volume34
Pages9413-23
AuthorsHayashi H, Kagamiyama H
TitleReaction of aspartate aminotransferase with L-erythro-3-hydroxyaspartate: involvement of Tyr70 in stabilization of the catalytic intermediates.
[34]
CommentsX-ray crystallography
PubMed ID7819232
JournalBiochemistry
Year1995
Volume34
Pages405-14
AuthorsMalashkevich VN, Jager J, Ziak M, Sauder U, Gehring H, Christen P, Jansonius JN
TitleStructural basis for the catalytic activity of aspartate aminotransferase K258H lacking the pyridoxal 5'-phosphate-binding lysine residue.
Related PDB1aia,1aib,1aic,1aka,1akb,1akc
[35]
CommentsX-ray crystallography
PubMed ID7556224
JournalEur J Biochem
Year1995
Volume232
Pages686-90
AuthorsGraber R, Kasper P, Malashkevich VN, Sandmeier E, Berger P, Gehring H, Jansonius JN, Christen P
TitleChanging the reaction specificity of a pyridoxal-5'-phosphate-dependent enzyme.
Related PDB1arg,1arh
[36]
CommentsX-ray crystallography
PubMed ID7851426
JournalEur J Biochem
Year1995
Volume227
Pages481-7
AuthorsVacca RA, Christen P, Malashkevich VN, Jansonius JN, Sandmeier E
TitleSubstitution of apolar residues in the active site of aspartate aminotransferase by histidine. Effects on reaction and substrate specificity.
Related PDB1ari
[37]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS)
Medline ID95205406
PubMed ID7897655
JournalJ Mol Biol
Year1995
Volume247
Pages111-24
AuthorsMalashkevich VN, Strokopytov BV, Borisov VV, Dauter Z, Wilson KS, Torchinsky YM
TitleCrystal structure of the closed form of chicken cytosolic aspartate aminotransferase at 1.9 A resolution.
Related PDB2cst
Related Swiss-protP00504
[38]
CommentsX-ray crystallography
PubMed ID7664122
JournalNat Struct Biol
Year1995
Volume2
Pages548-53
AuthorsMalashkevich VN, Onuffer JJ, Kirsch JF, Jansonius JN
TitleAlternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase.
Related PDB1ahe,1ahf,1ahg,1ahx,1ahy
[39]
CommentsX-ray crystallography
PubMed ID8952476
JournalBiochemistry
Year1996
Volume35
Pages15260-8
Authorsvon Stosch AG
TitleAspartate aminotransferase complexed with erythro-beta-hydroxyaspartate: crystallographic and spectroscopic identification of the carbinolamine intermediate.
Related PDB1ivr
[40]
PubMed ID8856080
JournalEur J Biochem
Year1996
Volume240
Pages751-5
AuthorsKasper P, Sterk M, Christen P, Gehring H
TitleMolecular-dynamics simulation of domain movements in aspartate aminotransferase.
[41]
CommentsX-ray crystallography
PubMed ID8665890
JournalEur J Biochem
Year1996
Volume236
Pages1025-32
AuthorsMarkovic-Housley Z, Schirmer T, Hohenester E, Khomutov AR, Khomutov RM, Karpeisky MY, Sandmeier E, Christen P, Jansonius JN
TitleCrystal structures and solution studies of oxime adducts of mitochondrial aspartate aminotransferase.
Related PDB1oxo,1oxp
[42]
PubMed ID9012676
JournalBiochemistry
Year1997
Volume36
Pages615-25
AuthorsMollova ET, Metzler DE, Kintanar A, Kagamiyama H, Hayashi H, Hirotsu K, Miyahara I
TitleUse of 1H-15N heteronuclear multiple-quantum coherence NMR spectroscopy to study the active site of aspartate aminotransferase.
[43]
CommentsX-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS)
Medline ID97362209
PubMed ID9211866
JournalJ Biol Chem
Year1997
Volume272
Pages17293-302
AuthorsRhee S, Silva MM, Hyde CC, Rogers PH, Metzler CM, Metzler DE, Arnone A
TitleRefinement and comparisons of the crystal structures of pig cytosolic aspartate aminotransferase and its complex with 2-methylaspartate.
Related PDB1ajr,1ajs
Related Swiss-protP00503
[44]
PubMed ID9761867
JournalActa Crystallogr D Biol Crystallogr
Year1998
Volume54
Pages659-61
AuthorsJeffery CJ, Barry T, Doonan S, Petsko GA, Ringe D
TitleCrystallization and preliminary X-ray diffraction analysis of aspartate aminotransferase from Saccharomyces cerevisiae.
[45]
PubMed ID9757130
JournalActa Crystallogr D Biol Crystallogr
Year1998
Volume54
Pages1032-4
AuthorsNakai T, Okada K, Kawaguchi S, Kato R, Kuramitsu S, Hirotsu K
TitleCrystallization and preliminary X-ray characterization of aspartate aminotransferase from an extreme thermophile, Thermus thermophilus HB8.
[46]
PubMed ID9790670
JournalBiochemistry
Year1998
Volume37
Pages15076-85
AuthorsHayashi H, Mizuguchi H, Kagamiyama H
TitleThe imine-pyridine torsion of the pyridoxal 5'-phosphate Schiff base of aspartate aminotransferase lowers its pKa in the unliganded enzyme and is crucial for the successive increase in the pKa during catalysis.
[47]
PubMed ID9722549
JournalJ Biol Chem
Year1998
Volume273
Pages23191-202
AuthorsMattingly JR Jr, Torella C, Iriarte A, Martinez-Carrion M
TitleConformation of aspartate aminotransferase isozymes folding under different conditions probed by limited proteolysis.
[48]
PubMed ID9792664
JournalJ Biol Chem
Year1998
Volume273
Pages29554-64
AuthorsNobe Y, Kawaguchi S, Ura H, Nakai T, Hirotsu K, Kato R, Kuramitsu S
TitleThe novel substrate recognition mechanism utilized by aspartate aminotransferase of the extreme thermophile Thermus thermophilus HB8.
[49]
CommentsX-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS)
Medline ID98318048
PubMed ID9655342
JournalProtein Sci
Year1998
Volume7
Pages1380-7
AuthorsJeffery CJ, Barry T, Doonan S, Petsko GA, Ringe D
TitleCrystal structure of Saccharomyces cerevisiae cytosolic aspartate aminotransferase.
Related PDB1yaa
Related Swiss-protP23542
[50]
CommentsX-ray crystallography
PubMed ID9893985
JournalBiochemistry
Year1999
Volume38
Pages905-13
AuthorsBirolo L, Malashkevich VN, Capitani G, De Luca F, Moretta A, Jansonius JN, Marino G
TitleFunctional and structural analysis of cis-proline mutants of Escherichia coli aspartate aminotransferase.
Related PDB1bqa,1bqd
[51]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)
Medline ID99155214
PubMed ID10029535
JournalBiochemistry
Year1999
Volume38
Pages2413-24
AuthorsNakai T, Okada K, Akutsu S, Miyahara I, Kawaguchi S, Kato R, Kuramitsu S, Hirotsu K
TitleStructure of Thermus thermophilus HB8 aspartate aminotransferase and its complex with maleate.
Related PDB1bjw,1bkg
Related Swiss-protQ56232
[52]
PubMed ID10556573
JournalBiochim Biophys Acta
Year1999
Volume1434
Pages191-201
AuthorsMahon MM, Graber R, Christen P, Malthouse JP
TitleThe aspartate aminotransferase-catalysed exchange of the alpha-protons of aspartate and glutamate: the effects of the R386A and R292V mutations on this exchange reaction.
[53]
PubMed ID10531314
JournalJ Biol Chem
Year1999
Volume274
Pages31203-8
AuthorsGraber R, Kasper P, Malashkevich VN, Strop P, Gehring H, Jansonius JN, Christen P
TitleConversion of aspartate aminotransferase into an L-aspartate beta-decarboxylase by a triple active-site mutation.
[54]
PubMed ID9880502
JournalJ Biol Chem
Year1999
Volume274
Pages1320-5
AuthorsMouratou B, Kasper P, Gehring H, Christen P
TitleConversion of tyrosine phenol-lyase to dicarboxylic amino acid beta-lyase, an enzyme not found in nature.
[55]
CommentsX-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT
Medline ID99107891
PubMed ID9891001
JournalJ Biol Chem
Year1999
Volume274
Pages2344-9
AuthorsOue S, Okamoto A, Yano T, Kagamiyama H
TitleRedesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues.
Related PDB1yoo
Related Swiss-protP00509
[56]
CommentsX-ray crystallography
PubMed ID10731702
JournalJ Biochem (Tokyo)
Year2000
Volume127
Pages337-43
AuthorsOue S, Okamoto A, Yano T, Kagamiyama H
TitleCocrystallization of a mutant aspartate aminotransferase with a C5-dicarboxylic substrate analog: structural comparison with the enzyme-C4-dicarboxylic analog complex.
Related PDB1czc,1cze
[57]
CommentsX-ray crystallography
PubMed ID10858450
JournalJ Biol Chem
Year2000
Volume275
Pages18939-45
AuthorsIshijima J, Nakai T, Kawaguchi S, Hirotsu K, Kuramitsu S
TitleFree energy requirement for domain movement of an enzyme.
Related PDB1c9c,1cq6,1cq7,1cq8
[58]
CommentsX-ray crystallography
PubMed ID10708649
JournalProtein Eng
Year2000
Volume13
Pages105-12
AuthorsJeffery CJ, Gloss LM, Petsko GA, Ringe D
TitleThe role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase.
Related PDB1b4x,1qir,1qis,1qit,5eaa
[59]
CommentsX-ray crystallography
PubMed ID11148029
JournalBiochemistry
Year2001
Volume40
Pages353-60
AuthorsMizuguchi H, Hayashi H, Okada K, Miyahara I, Hirotsu K, Kagamiyama H
TitleStrain is more important than electrostatic interaction in controlling the pKa of the catalytic group in aspartate aminotransferase.
Related PDB1g4v,1g4x,1g7w,1g7x
[60]
PubMed ID11432784
JournalJ Biochem (Tokyo)
Year2001
Volume130
Pages89-98
AuthorsUra H, Nakai T, Kawaguchi SI, Miyahara I, Hirotsu K, Kuramitsu S
TitleSubstrate recognition mechanism of thermophilic dual-substrate enzyme.
[61]
CommentsX-ray crystallography
PubMed ID12488449
JournalJ Biol Chem
Year2003
Volume278
Pages9481-8
AuthorsHayashi H, Mizuguchi H, Miyahara I, Nakajima Y, Hirotsu K, Kagamiyama H
TitleConformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysis.
Related PDB1ix6,1ix7,1ix8

comments
This enzyme belongs to the Aspartate aminotransferase (AAT) subclass of type-I PLP-dependent enzyme superfamily (Aspartate aminotransferase superfamily; AAT).
This enzyme catalyzes transamination, which is composed of the following reactions:
(A) Formation of external aldimine (with amine group of L-Aspartate),
(B) Isomerization (change in the position of double-bond), forming a ketimine intermediate.
(C) Schiff-base deforming by hydration, releasing the first product, oxaloacetate, and PMP.
(D) Schiff-base forming of PMP with carbonyl group of the second substrate, 2-oxoglutarate, leading again to a ketimine intermediate.
(E) Isomerization (change in the position of double-bond).
(F) Formation of internal aldimine, leading to the elimination of the product from PLP.
These reactions proceed in the following way:
(A) Formation of external aldimine (with amine group of L-Aspartate) (see [11], [13], [18] & [46])
(A1) Tyr225 interacts with O3' atom of PLP, when the PLP-aldimine is protonated, modulating and keeping the O3' of PLP negatively charged (see [13]).
(A2) The negatively charged O3 atom of PLP modulates the pKa of the alpha-amino group of substrate, L-aspartate, and also the pKa of the internal aldimine with Lys258. Here, according to the literature [46], [59] & [61], the imine-pyridine torsion (or strain) of PLP-Schiff base lowers pKa of the internal aldimine, without lowering the external aldimine. In any case, the difference in the pKa values facilitates the proton transfer from the alpha-amino group of L-aspartate to the NZ nitrogen of Lys258.
(A3) The deprotonated amine group of L-aspartate makes a nucleophilic attack on the C4' carbon of PLP, forming a transient geminal diamine intermediate.
(A4) There must be a general base, which deprotonates the amine group of the previously L-aspartate substrate, so that the lone pair of the amine group can attack on the C4' atom to form a double-bond, and to release the amine of the catalytic residue, Lys258. Considering the active-site structure, Tyr70' (from the adjacent chain) may play the role as the general base, although the literature has not mentioned it (except for the literature [11]). (The released Lys258 must be deprotonated, so that it can act as a general base at the next stage.)
(A5) The reaction produces the external aldimine with L-aspartate.
(B) Isomerization (change in the position of double-bond), forming a ketimine intermediate (see [17], [18], [20], [21], [22] & [24]).
(B1) Asp222 interacts with the N1 atom of PLP, modulating and enhancing the activity of the PLP cofactor as an electron sink, which facilitates the abstraction of alpha-proton from the aspartate covalently bound to the PLP (see [17] & [24]). At the same time, Tyr225 also interacts with the O3' atom of the PLP, modulating the activity of the PLP (see [13]).
(B2) Lys258 acts as a general base to deprotonate the alpha-proton of the amino acid substrate, forming a quinonoid intermediate.
(B3) Lys258 acts as a general acid to protonate the C4' atom of the PLP, leading to the formation of a ketimine intermediate.
(C) Schiff-base deforming by hydration, releasing the first product, oxaloacetate, and PMP (see [18] & [26]).
(C1) Lys258 acts as a general base to activate a water (at the si-face side of cofactor).
(C2) The activated water molecule makes a nucleophilic attack on the alpha-carbon atom of the substrate (from the si-face side), forming a carbinolamine intermediate.
(C3) Lys258 may act as a general acid to protonate the N4' atom of the PLP. Tyr225 may modulate the activity of Lys258. (Tyr225 is hydrogen-bonded to the O3 atom of the PLP).
(C4) The lone pair of the hydroxyl oxygen makes a nucleophilic attack on the C4' atom, whereas Lys258 acts as a general base to deprotonate the hydroxyl group, releasing the first product, oxaloacetate and the PMP.
(D) Schiff-base forming of PMP with carbonyl group of the second substrate (see [18] & [26])
(D1) The second substrate, 2-oxoglutarate, is bound to the active site, with the carbonyl oxygen hydrogen-bonded by Lys258.
(D2) The amine group (or the N4' atom) of PMP is unprotonated and makes a nucleophilic attack on the carbonyl carbon of the substrate, whereas Lys258 acts as a general acid to protonate the carbonyl oxygen, forming a carbinolamine intermediate.
(D3) Lys258 acts as a general base to deprotonate the N4 amine group. Tyr225 may modulate the activity of Lys258. (Tyr225 is hydrogen-bonded to the O3 atom of the PLP).
(D4) The lone pair of the N4' nitrogen atom makes a nucleophilic attack on the carbon atom, whereas Lys258 acts as a general acid to the hydroxyl group of the carbinolamine intermediate, leading to the cleavage between the carbon and the N4' atom, and to the release of a water moleucle. This reaction gives a ketimine intermediate again.
(E) Isomerization (change in the position of double-bond): (Inverse reaction of (B))
(E1) Asp222 modulates and enhances the activity of the PLP cofactor as an electron sink, which facilitates the abstraction of alpha-proton from the C4' atom of the PLP.
(E2) Lys258 acts as a general base to deprotonate the C4' atom of the PLP, leading to the formation of a quinonoid intermediate.
(E3) Lys258 acts as a general acid to protonate the alpha-proton of the amino acid substrate, forming an external aldimine. (As a result, Lys258 must be deprotonated, so that it can act as a general base at the next stage.)
(F) Formation of internal aldimine, leading to the elimination of the product from PLP: (Inverse reaction of (A))
(F1) Tyr225 interacts with O3' atom of PLP, when the PLP-aldimine is protonated, modulating and keeping the O3' of PLP negatively charged (see [13]).
(F2) The deprotonated amine group of Lys258 makes a nucleophilic attack on the C4' carbon of the PLP of the external aldimine, forming a transient geminal diamine intermediate. On the other hand, there must be a general acid, which protonates the N4' nitrogen atom of the external aldimine or the geminal diamine. Considering the active-site structure, Tyr70' (from the adjacent chain) may play the role as the general acid, although the literature has not mentioned it (except for the literature [11]).
(F3) The lone pair of the amine nitrogen of Lys258 can attack on the C4' atom to form a double-bond, and to release the amine of the second product, L-glutamate.
(F4) The negatively charged O3 atom of PLP modulates the pKa of the alpha-amino group of product, L-glutamate, and also the pKa of the internal aldimine with Lys258. In any case, the difference in the pKa values facilitates the proton transfer from the NZ nitrogen of Lys258 to the alpha-amine group of L-glutarate.
The pKas of the related groups are as follows (see [46]):
Unliganded internal aldimine; 6.8
Internal aldimine complexed with substrate/product; 8.1
External aldimine; 10.2

createdupdated
2004-10-212009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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