EzCatDB: T00089

DB codeT00089
RLCP classification5.161.586000.968
6.30.83700.5070
8.12111.711000.5510
5.14.3250000.5471
4.1164.693000.5470
8.11211.912000.5510
6.40.477300.5510
CATH domainDomain 13.20.20.70Catalytic domain
Domain 23.40.50.1100Catalytic domain
Domain 33.40.50.1100Catalytic domain
E.C.4.2.1.20
CSA1a50,1geq

CATH domainRelated DB codes (homologues)
3.20.20.70S00215,S00217,S00218,S00219,S00532,S00198,S00220,S00745,S00537,S00538,S00539,S00826,S00841,S00235,S00239,S00240,S00243,S00244,S00199,S00200,S00201,S00221,S00222,S00847,S00224,S00225,S00226,D00014,D00029,M00141,T00015,T00239,D00664,D00665,D00804,D00863
3.40.50.1100D00264,T00088

Enzyme Name
Swiss-protKEGG

Q8U094P00929Q8U093Q8U0J5P0A2K1
Protein nameTryptophan synthase alpha chainTryptophan synthase alpha chainTryptophan synthase beta chain 1Tryptophan synthase beta chain 2Tryptophan synthase beta chaintryptophan synthase
L-tryptophan synthetase
indoleglycerol phosphate aldolase
tryptophan desmolase
tryptophan synthetase
L-serine hydro-lyase (adding indoleglycerol-phosphate)
SynonymsEC 4.2.1.20
EC 4.2.1.20
EC 4.2.1.20
EC 4.2.1.20
EC 4.2.1.20

KEGG pathways
MAP codePathways
MAP00400Phenylalanine, tyrosine and tryptophan biosynthesis

Swiss-prot:Accession NumberQ8U094P00929Q8U093Q8U0J5P0A2K1
Entry nameTRPA_PYRFUTRPA_SALTYTRPB1_PYRFUTRPB2_PYRFUTRPB_SALTY
ActivityL-serine + 1-C-(indol-3-yl)glycerol 3- phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H(2)O.L-serine + 1-C-(indol-3-yl)glycerol 3- phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H(2)O.L-serine + 1-C-(indol-3-yl)glycerol 3- phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H(2)O.L-serine + 1-C-(indol-3-yl)glycerol 3- phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H(2)O.L-serine + 1-C-(indol-3-yl)glycerol 3- phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H(2)O.
SubunitTetramer of two alpha and two beta chains (By similarity).Tetramer of two alpha and two beta chains.Tetramer of two alpha and two beta chains (By similarity).Tetramer of two alpha and two beta chains (By similarity).Tetramer of two alpha and two beta chains.
Subcellular location




Cofactor

Pyridoxal phosphate (By similarity).Pyridoxal phosphate (By similarity).Pyridoxal phosphate.


CofactorsSubstratesProductsintermediates
KEGG-idC00018C99999C00065C03506C00078C00118C00001C00463




CompoundPyridoxal phosphateMonovalent ionL-Serine1-(Indol-3-yl)glycerol 3-phosphateL-TryptophanD-Glyceraldehyde 3-phosphateH2OIndoleExternal aldimine intermediate Quinonoid Intermediate-1Aminoacrylate intermediateQuinonoid Intermediate-2External aldimine intermeidate
Typearomatic ring (with nitrogen atoms),phosphate group/phosphate ionorganic ionamino acids,carbohydratearomatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,phosphate group/phosphate ionamino acids,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms)carbohydrate,phosphate group/phosphate ionH2O





1geqAUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1geqBUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1a50AUnboundUnboundUnboundAnalogue:FIPUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1a5aAUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1a5bAUnboundUnboundUnboundBound:IGPUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1a5sAUnboundUnboundUnboundAnalogue:FIPUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1beuAUnboundUnboundUnboundAnalogue:IPLUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1bksAUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1c29AUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1c8vAUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1c9dAUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1cw2AUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1cx9AUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1fuyAUnboundUnboundUnboundAnalogue:FIPUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1k3uAUnboundUnboundUnboundAnalogue:IADUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1k7eAUnboundUnboundUnboundAnalogue:IAGUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1k7fAUnboundUnboundUnboundAnalogue:IAVUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1k8xAUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1k8yAUnboundUnboundUnboundUnboundUnboundBound:13P
UnboundUnboundUnboundUnboundUnboundUnbound
1k8zAUnboundUnboundUnboundAnalogue:IAGUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1kfbAUnboundUnboundUnboundBound:IGPUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1kfcAUnboundUnboundUnboundAnalogue:IPLUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1kfeAUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1kfjAUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1kfkAUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1qopAUnboundUnboundUnboundAnalogue:IPLUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1qoqAUnboundUnboundUnboundBound:IGPUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1ttpAUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1ttqAUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1ubsAUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1wsyAUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
2trsAUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
2tsyAUnboundUnboundUnboundUnboundUnboundBound:G3P
UnboundUnboundUnboundUnboundUnboundUnbound
2tysAUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
2wsyAUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1a50B01Bound:PLPUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1a5aB01Bound:PLPUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1a5bB01Bound:PLPUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1a5sB01Bound:PLPUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundIntermediate-bound:PLP-SERUnboundUnbound
1beuB01Analogue:PLSUnboundUnboundUnboundUnboundUnbound
UnboundIntermediate-bound:PLSUnboundUnboundUnboundUnbound
1bksB01Bound:PLPUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1c29B01Bound:PLPUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1c8vB01Bound:PLPUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1c9dB01Bound:PLPUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1cw2B01Bound:PLPUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1cx9B01Bound:PLPUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1fuyB01Bound:PLPUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1k3uB01Bound:PLPUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1k7eB01Bound:PLPUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1k7fB01Bound:PLPUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1k8xB01Bound:PLPUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1k8yB01Bound:PLPUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1k8zB01Bound:PLPUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1kfbB01Bound:PLPUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1kfcB01Bound:PLPUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1kfeB01Analogue:PLSUnboundUnboundUnboundUnboundUnbound
UnboundIntermediate-bound:PLSUnboundUnboundUnboundUnbound
1kfjB01Analogue:PLSUnboundUnboundUnboundUnboundUnbound
UnboundIntermediate-bound:PLSUnboundUnboundUnboundUnbound
1kfkB01Bound:PLPUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1qopB01Bound:PLPUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1qoqB01Bound:PLPUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1ttpB01Bound:PLPUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1ttqB01Bound:PLPUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1ubsB01Bound:PLPUnboundUnboundUnboundUnboundUnbound
UnboundIntermediate-bound:PLP-SERUnboundUnboundUnboundUnbound
1wsyB01Bound:PLPUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
2trsB01Analogue:PLSUnboundUnboundUnboundUnboundUnbound
UnboundIntermediate-bound:PLSUnboundUnboundUnboundUnbound
2tsyB01Analogue:PLSUnboundUnboundUnboundUnboundUnbound
UnboundIntermediate-bound:PLSUnboundUnboundUnboundUnbound
2tysB01Analogue:PLTUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundIntermediate-bound:PLT
2wsyB01Bound:PLPUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1a50B02UnboundBound:_NAUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1a5aB02UnboundBound:__KUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1a5bB02UnboundBound:__KUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1a5sB02UnboundBound:_NAUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1beuB02UnboundBound:__KUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1bksB02UnboundBound:_NAUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1c29B02UnboundBound:_NAUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1c8vB02UnboundBound:_NAUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1c9dB02UnboundBound:_NAUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1cw2B02UnboundBound:_NAUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1cx9B02UnboundBound:_NAUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1fuyB02UnboundBound:_NAUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1k3uB02UnboundBound:_NAUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1k7eB02UnboundBound:_NAUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1k7fB02UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1k8xB02UnboundBound:_NAUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1k8yB02UnboundBound:_NAUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1k8zB02UnboundBound:_NAUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1kfbB02UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1kfcB02UnboundBound:_NAUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1kfeB02UnboundBound:_NAUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1kfjB02UnboundBound:_NAUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1kfkB02UnboundBound:_NAUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1qopB02UnboundBound:_NAUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1qoqB02UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1ttpB02UnboundBound:_CSUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1ttqB02UnboundBound:__KUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1ubsB02UnboundBound:_NAUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
1wsyB02UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
2trsB02UnboundBound:_NAUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
2tsyB02UnboundBound:_NAUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
2tysB02UnboundBound:_NAUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound
2wsyB02UnboundBound:_NAUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P00929 & PDB;1bks, 1qoq, 1ttp, 1ttq
pdbCatalytic residuesCofactor-binding residuescomment
1geqAGLU 36;ASP 47;       

invisible 167-173
1geqBGLU 36;ASP 47;THR 168

invisible 170-172
1a50AGLU 49;ASP 60;THR 183


1a5aAGLU 49;      ;       

mutant D60N, invisible 177-189
1a5bAGLU 49;      ;       

mutant D60N, invisible 177-195
1a5sAGLU 49;ASP 60;THR 183


1beuAGLU 49;      ;       

mutant D60N, invisible 177-191
1bksAGLU 49;ASP 60;       

invisible 178-189
1c29AGLU 49;ASP 60;THR 183


1c8vAGLU 49;ASP 60;THR 183


1c9dAGLU 49;ASP 60;THR 183


1cw2AGLU 49;ASP 60;THR 183


1cx9AGLU 49;ASP 60;THR 183


1fuyAGLU 49;ASP 60;THR 183


1k3uAGLU 49;ASP 60;THR 183


1k7eAGLU 49;ASP 60;THR 183


1k7fAGLU 49;ASP 60;       

invisible 179-192
1k8xAGLU 49;ASP 60;       

mutant T183V, invisible 178-195
1k8yAGLU 49;ASP 60;       

mutant S178P, invisible 179-191
1k8zAGLU 49;ASP 60;       

mutant S178P, invisible 179-189
1kfbAGLU 49;ASP 60;       

mutant T183V, invisivle 180-192
1kfcAGLU 49;ASP 60;       

mutant T183V, invisivle 179-192
1kfeAGLU 49;ASP 60;       

mutant T183V, invisivle 178-193
1kfjAGLU 49;ASP 60;       

invisible 178-191
1kfkAGLU 49;ASP 60;       

invisible 178-193
1qopAGLU 49;ASP 60;THR 183


1qoqAGLU 49;ASP 60;       

invisible 179-192
1ttpAGLU 49;ASP 60;       

invisible 178-189
1ttqAGLU 49;ASP 60;       

invisible 178-189
1ubsAGLU 49;ASP 60;       

invisible 181-191
1wsyAGLU 49;ASP 60;       

invisible 178-191
2trsAGLU 49;ASP 60;THR 183


2tsyAGLU 49;ASP 60;THR 183


2tysAGLU 49;ASP 60;       

invisible 179-191
2wsyAGLU 49;      ;       

 invisible 54-62, 177-195
1a50B01LYS 87;GLU 109
LYS 87(PLP binding)

1a5aB01LYS 87;GLU 109
LYS 87(PLP binding)

1a5bB01LYS 87;GLU 109
LYS 87(PLP binding)

1a5sB01LYS 87;GLU 109
LYS 87(PLP binding)

1beuB01LYS 87;GLU 109
LYS 87(PLP binding)

1bksB01LYS 87;GLU 109
LYS 87(PLP binding)

1c29B01LYS 87;GLU 109
LYS 87(PLP binding)

1c8vB01LYS 87;GLU 109
LYS 87(PLP binding)

1c9dB01LYS 87;GLU 109
LYS 87(PLP binding)

1cw2B01LYS 87;GLU 109
LYS 87(PLP binding)

1cx9B01LYS 87;GLU 109
LYS 87(PLP binding)

1fuyB01LYS 87;GLU 109
LYS 87(PLP binding)

1k3uB01LYS 87;GLU 109
LYS 87(PLP binding)

1k7eB01LYS 87;GLU 109
LYS 87(PLP binding)

1k7fB01LYS 87;GLU 109
LYS 87(PLP binding)

1k8xB01LYS 87;GLU 109
LYS 87(PLP binding)

1k8yB01LYS 87;GLU 109
LYS 87(PLP binding)

1k8zB01LYS 87;GLU 109
LYS 87(PLP binding)

1kfbB01LYS 87;GLU 109
LYS 87(PLP binding)

1kfcB01LYS 87;GLU 109
LYS 87(PLP binding)

1kfeB01LYS 87;GLU 109
LYS 87(PLP binding)

1kfjB01LYS 87;GLU 109
LYS 87(PLP binding)

1kfkB01LYS 87;GLU 109
LYS 87(PLP binding)

1qopB01LYS 87;GLU 109
LYS 87(PLP binding)

1qoqB01LYS 87;GLU 109
LYS 87(PLP binding)

1ttpB01LYS 87;GLU 109
LYS 87(PLP binding)

1ttqB01LYS 87;GLU 109
LYS 87(PLP binding)

1ubsB01      ;GLU 109
                   
mutant K87T
1wsyB01LYS 87;GLU 109
LYS 87(PLP binding)

2trsB01      ;GLU 109
                   
mutant K87T
2tsyB01      ;GLU 109
                   
mutant K87T
2tysB01      ;GLU 109
                   
mutant K87T
2wsyB01LYS 87;GLU 109
LYS 87(PLP binding)

1a50B02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

1a5aB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

1a5bB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

1a5sB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

1beuB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

1bksB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

1c29B02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

1c8vB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

1c9dB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

1cw2B02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

1cx9B02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

1fuyB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)
mutant A169L;C170W
1k3uB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

1k7eB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

1k7fB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

1k8xB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

1k8yB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

1k8zB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

1kfbB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

1kfcB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

1kfeB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

1kfjB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

1kfkB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

1qopB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

1qoqB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

1ttpB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

1ttqB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

1ubsB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

1wsyB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

2trsB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

2tsyB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

2tysB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)

2wsyB02HIS 86;ASP 305
GLY 232;PHE 306;SER 308(Monovalent ion binding)


References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]p.28-30
[5]Fig.15, Fig.16, Fig.17, Fig.18, Fig.19, p.128-151
[11]Scheme I, Scheme II, p.11859
[12]Scheme I, Fig.1, p.3836-38389
[16]Scheme I, p.87338
[17]FIG. 1, p.14930-149318
[21]Scheme 1, p.9473-94759
[22]SCHEME I, p.17336-173375
[25]Scheme 1, p.738411
[26]Scheme 111
[29]Scheme 1A, Fig.11, p.7674-7678
[32]Figure 110
[34]Scheme 110
[35]Scheme 1B5
[36]FIGURE 25
[38]SCHEME 1, p.85552
[39]SCHEME 1, p.332527
[42]Fig.1, p.12672-126732
[43]p.16479
[44]Scheme 1, p.7134-714110
[45]Scheme 1, p.7127-71296
[46]SCHEME 1, p.31191-311949
[48]Fig.3, Fig.9, p.118-124, p.127-132
[52]Scheme 1, p.7430-74326
[54]Scheme 17
[55]Scheme 1, Scheme 2, p.9998-100006
[59]Fig.1

references
[1]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Medline ID89034326
PubMed ID3053720
JournalJ Biol Chem
Year1988
Volume263
Pages17857-71
AuthorsHyde CC, Ahmed SA, Padlan EA, Miles EW, Davies DR
TitleThree-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium.
Related Swiss-protP00929,P0A2K1
[2]
PubMed ID1366510
JournalBiotechnology (N Y)
Year1990
Volume8
Pages27-32
AuthorsHyde CC, Miles EW
TitleThe tryptophan synthase multienzyme complex: exploring structure-function relationships with X-ray crystallography and mutagenesis.
[3]
PubMed ID2190828
JournalEur J Biochem
Year1990
Volume189
Pages667-73
AuthorsSawada S, Akutsu H, Ogasahara K, Yutani K
TitleAssignment of tyrosine resonances in the 1H-NMR spectrum of tryptophan synthase alpha-subunit. Monitoring conformational changes due to substitutions at position 49.
[4]
PubMed ID1692319
JournalJ Biol Chem
Year1990
Volume265
Pages7987-93
AuthorsMurry-Brelier A, Goldberg ME
TitleMechanism of inactivation of the beta 2 subunit of Escherichia coli tryptophan synthase by monoclonal antibodies.
[5]
PubMed ID2053470
JournalAdv Enzymol Relat Areas Mol Biol
Year1991
Volume64
Pages93-172
AuthorsMiles EW
TitleStructural basis for catalysis by tryptophan synthase.
[6]
PubMed ID1849406
JournalBiochem J
Year1991
Volume274
Pages807-12
AuthorsMalthouse JP, Milne JJ, Gariani LS
TitleA comparative study of the kinetics and stereochemistry of the serine hydroxymethyltransferase- and tryptophan synthase-catalysed exchange of the pro-2R and pro-2S protons of glycine.
[7]
PubMed ID1868082
JournalBiochemistry
Year1991
Volume30
Pages8067-74
AuthorsChaffotte A, Guillou Y, Delepierre M, Hinz HJ, Goldberg ME
TitleThe isolated C-terminal (F2) fragment of the Escherichia coli tryptophan synthase beta 2-subunit folds into a stable, organized nonnative conformation.
[8]
PubMed ID2021608
JournalBiochemistry
Year1991
Volume30
Pages4173-9
AuthorsKaufmann M, Schwarz T, Jaenicke R, Schnackerz KD, Meyer HE, Bartholmes P
TitleLimited proteolysis of the beta 2-dimer of tryptophan synthase yields an enzymatically active derivative that binds alpha-subunits.
[9]
PubMed ID1718750
JournalEur J Biochem
Year1991
Volume201
Pages681-93
AuthorsDelepierre M, Larvor MP, Baleux F, Goldberg ME
Title1H-NMR conformational analysis of a high-affinity antigenic 11-residue peptide from the tryptophan synthase beta 2 subunit.
[10]
PubMed ID1939081
JournalJ Biol Chem
Year1991
Volume266
Pages20205-12
AuthorsLim WK, Sarkar SK, Hardman JK
TitleEnzymatic properties of mutant Escherichia coli tryptophan synthase alpha-subunits.
[11]
PubMed ID1346502
JournalBiochemistry
Year1992
Volume31
Pages1180-90
AuthorsBrzovic PS, Kayastha AM, Miles EW, Dunn MF
TitleSubstitution of glutamic acid 109 by aspartic acid alters the substrate specificity and catalytic activity of the beta-subunit in the tryptophan synthase bienzyme complex from Salmonella typhimurium.
[12]
PubMed ID1567839
JournalBiochemistry
Year1992
Volume31
Pages3831-9
AuthorsBrzovic PS, Ngo K, Dunn MF
TitleAllosteric interactions coordinate catalytic activity between successive metabolic enzymes in the tryptophan synthase bienzyme complex.
[13]
PubMed ID1559990
JournalJ Biol Chem
Year1992
Volume267
Pages7520-8
AuthorsYang XJ, Miles EW
TitleThreonine 183 and adjacent flexible loop residues in the tryptophan synthase alpha subunit have critical roles in modulating the enzymatic activities of the beta subunit in the alpha 2 beta 2 complex.
[14]
PubMed ID1309752
JournalJ Biol Chem
Year1992
Volume267
Pages526-41
AuthorsZhao GP, Somerville RL
TitleGenetic and biochemical characterization of the trpB8 mutation of Escherichia coli tryptophan synthase. An amino acid switch at the sharp turn of the trypsin-sensitive "hinge" region diminishes substrate binding and alters solubility.
[15]
PubMed ID8268176
JournalBiochemistry
Year1993
Volume32
Pages13981-90
AuthorsSaab-Rincon G, Froebe CL, Matthews CR
TitleUrea-induced unfolding of the alpha subunit of tryptophan synthase: one-dimensional proton NMR evidence for residual structure near histidine-92 at high denaturant concentration.
[16]
PubMed ID8473317
JournalJ Biol Chem
Year1993
Volume268
Pages8727-34
AuthorsLu Z, Nagata S, McPhie P, Miles EW
TitleLysine 87 in the beta subunit of tryptophan synthase that forms an internal aldimine with pyridoxal phosphate serves critical roles in transimination, catalysis, and product release.
[17]
PubMed ID8325869
JournalJ Biol Chem
Year1993
Volume268
Pages14921-31
AuthorsZhao GP, Somerville RL
TitleA single amino acid switch within the "hinge" region of the tryptophan synthase beta subunit of Escherichia coli that leads to diminished association with alpha subunit and arrested conversion of ESII to product.
[18]
PubMed ID8206268
JournalBiochem Soc Trans
Year1994
Volume22
Pages43S
AuthorsMilne JJ, Malthouse JP
TitleA study of the tryptophan synthase catalysed H/D exchange of the alpha-protons of amino acids.
[19]
PubMed ID7929385
JournalJ Biol Chem
Year1994
Volume269
Pages26591-3
AuthorsSchlichting I, Yang XJ, Miles EW, Kim AY, Anderson KS
TitleStructural and kinetic analysis of a channel-impaired mutant of tryptophan synthase.
[20]
PubMed ID7487918
JournalBiochem J
Year1995
Volume311
Pages1015-9
AuthorsMilne JJ, Malthouse JP
TitleFactors affecting the stereospecificity and catalytic efficiency of the tryptophan synthase-catalysed exchange of the pro-2R and pro-2S protons of glycine.
[21]
PubMed ID7626617
JournalBiochemistry
Year1995
Volume34
Pages9466-76
AuthorsWoehl EU, Dunn MF
TitleMonovalent metal ions play an essential role in catalysis and intersubunit communication in the tryptophan synthase bienzyme complex.
[22]
PubMed ID7615535
JournalJ Biol Chem
Year1995
Volume270
Pages17333-8
AuthorsRuvinov SB, Ahmed SA, McPhie P, Miles EW
TitleMonovalent cations partially repair a conformational defect in a mutant tryptophan synthase alpha 2 beta 2 complex (beta-E109A).
[23]
PubMed ID8615770
JournalBiochem J
Year1996
Volume314
Pages787-91
AuthorsMilne JJ, Malthouse JP
TitleThe effect of different amino acid side chains on the stereospecificity and catalytic efficiency of the tryptophan synthase-catalysed exchange of the alpha-protons of amino acids.
[24]
PubMed ID8674622
JournalBiochem Soc Trans
Year1996
Volume24
Pages133S
AuthorsMilne JJ, Malthouse JP
TitleEnzymatic synthesis of alpha-deuterated amino acids.
[25]
PubMed ID8652514
JournalBiochemistry
Year1996
Volume35
Pages7378-86
AuthorsHur O, Leja C, Dunn MF
TitleEvidence of a low-barrier hydrogen bond in the tryptophan synthase catalytic mechanism.
[26]
PubMed ID8664293
JournalBiochemistry
Year1996
Volume35
Pages5002-13
AuthorsPan P, Dunn MF
Titlebeta-Site covalent reactions trigger transitions between open and closed conformations of the tryptophan synthase bienzyme complex.
[27]
CommentsX-ray crystallography
PubMed ID8672457
JournalBiochemistry
Year1996
Volume35
Pages4211-21
AuthorsRhee S, Parris KD, Ahmed SA, Miles EW, Davies DR
TitleExchange of K+ or Cs+ for Na+ induces local and long-range changes in the three-dimensional structure of the tryptophan synthase alpha2beta2 complex.
Related PDB1ttp,1ttq,1ubs
[28]
PubMed ID8639683
JournalBiochemistry
Year1996
Volume35
Pages1988-94
AuthorsSaab-Rincon G, Gualfetti PJ, Matthews CR
TitleMutagenic and thermodynamic analyses of residual structure in the alpha subunit of tryptophan synthase.
[29]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medline ID97352620
PubMed ID9201907
JournalBiochemistry
Year1997
Volume36
Pages7664-80
AuthorsRhee S, Parris KD, Hyde CC, Ahmed SA, Miles EW, Davies DR
TitleCrystal structures of a mutant (betaK87T) tryptophan synthase alpha2beta2 complex with ligands bound to the active sites of the alpha- and beta-subunits reveal ligand-induced conformational changes.
Related PDB2trs,2tsy,2tys
Related Swiss-protP00929,P0A2K1
[30]
PubMed ID9220983
JournalBiochemistry
Year1997
Volume36
Pages8954-61
AuthorsRondard P, Bregegere F, Lecroisey A, Delepierre M, Bedouelle H
TitleConformational and functional properties of an undecapeptide epitope fused with the C-terminal end of the maltose binding protein.
[31]
PubMed ID9220984
JournalBiochemistry
Year1997
Volume36
Pages8962-8
AuthorsRondard P, Goldberg ME, Bedouelle H
TitleMutational analysis of an antigenic peptide shows recognition in a loop conformation.
[32]
PubMed ID9020588
JournalTrends Biochem Sci
Year1997
Volume22
Pages22-7
AuthorsPan P, Woehl E, Dunn MF
TitleProtein architecture, dynamics and allostery in tryptophan synthase channeling.
[33]
PubMed ID10909824
JournalBiochem Soc Trans
Year1998
Volume26
PagesS66
AuthorsMalthouse JP, Fitzpatrick TB, Mahon MM
TitleA comparison of some of the methods available for analysing the substrate dependence of the exchange of the alpha-protons of amino acids catalysed by pyridoxal-phosphate-dependent enzymes.
[34]
PubMed ID9772188
JournalBiochemistry
Year1998
Volume37
Pages14591-604
AuthorsJhee KH, McPhie P, Ro HS, Miles EW
TitleTryptophan synthase mutations that alter cofactor chemistry lead to mechanism-based inactivation.
[35]
PubMed ID9692955
JournalBiochemistry
Year1998
Volume37
Pages10653-9
AuthorsRhee S, Miles EW, Mozzarelli A, Davies DR
TitleCryocrystallography and microspectrophotometry of a mutant (alpha D60N) tryptophan synthase alpha 2 beta 2 complex reveals allosteric roles of alpha Asp60.
[36]
CommentsX-ray crystallography
PubMed ID9548921
JournalBiochemistry
Year1998
Volume37
Pages5394-406
AuthorsSchneider TR, Gerhardt E, Lee M, Liang PH, Anderson KS, Schlichting I
TitleLoop closure and intersubunit communication in tryptophan synthase.
Related PDB1a50,1a5s,2wsy
[37]
PubMed ID9700925
JournalBiophys Chem
Year1998
Volume73
Pages265-80
AuthorsKishore N, Tewari YB, Akers DL, Goldberg RN, Miles EW
TitleA thermodynamic investigation of reactions catalyzed by tryptophan synthase.
[38]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medline ID98204834
PubMed ID9535826
JournalJ Biol Chem
Year1998
Volume273
Pages8553-5
AuthorsRhee S, Miles EW, Davies DR
TitleCryo-crystallography of a true substrate, indole-3-glycerol phosphate, bound to a mutant (alphaD60N) tryptophan synthase alpha2beta2 complex reveals the correct orientation of active site alphaGlu49.
Related PDB1a5a,1a5b
Related Swiss-protP00929,P0A2K1
[39]
PubMed ID9837895
JournalJ Biol Chem
Year1998
Volume273
Pages33247-53
AuthorsSchnackerz KD, Mozzarelli A
TitlePlasticity of the tryptophan synthase active site probed by 31P NMR spectroscopy.
[40]
PubMed ID10090734
JournalBiochemistry
Year1999
Volume38
Pages3478-90
AuthorsBahar I, Jernigan RL
TitleCooperative fluctuations and subunit communication in tryptophan synthase.
[41]
PubMed ID10387029
JournalBiochemistry
Year1999
Volume38
Pages7881-90
AuthorsFan YX, McPhie P, Miles EW
TitleGuanidine hydrochloride exerts dual effects on the tryptophan synthase alpha 2 beta 2 complex as a cation activator and as a modulator of the active site conformation.
[42]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Medline ID99435740
PubMed ID10504236
JournalBiochemistry
Year1999
Volume38
Pages12665-74
AuthorsSachpatzidis A, Dealwis C, Lubetsky JB, Liang PH, Anderson KS, Lolis E
TitleCrystallographic studies of phosphonate-based alpha-reaction transition-state analogues complexed to tryptophan synthase.
Related PDB1c29,1c8v,1c9d,1cw2,1cx9
Related Swiss-protP00929,P0A2K1
[43]
CommentsX-ray crystallography
PubMed ID10600108
JournalBiochemistry
Year1999
Volume38
Pages16469-80
AuthorsWeyand M, Schlichting I
TitleCrystal structure of wild-type tryptophan synthase complexed with the natural substrate indole-3-glycerol phosphate.
Related PDB1qop,1qoq
[44]
PubMed ID10353823
JournalBiochemistry
Year1999
Volume38
Pages7131-41
AuthorsWoehl E, Dunn MF
TitleMechanisms of monovalent cation action in enzyme catalysis: the tryptophan synthase alpha-, beta-, and alpha beta-reactions.
[45]
PubMed ID10353822
JournalBiochemistry
Year1999
Volume38
Pages7118-30
AuthorsWoehl E, Dunn MF
TitleMechanisms of monovalent cation action in enzyme catalysis: the first stage of the tryptophan synthase beta-reaction.
[46]
PubMed ID10531312
JournalJ Biol Chem
Year1999
Volume274
Pages31189-94
AuthorsRo HS, Wilson Miles E
TitleCatalytic mechanism of the tryptophan synthase alpha(2)beta(2) complex. Effects of pH, isotopic substitution, and allosteric ligands.
[47]
PubMed ID10329177
JournalJ Mol Biol
Year1999
Volume288
Pages753-63
AuthorsMerz A, Knochel T, Jansonius JN, Kirschner K
TitleThe hyperthermostable indoleglycerol phosphate synthase from Thermotoga maritima is destabilized by mutational disruption of two solvent-exposed salt bridges.
[48]
PubMed ID10507003
JournalMethods Enzymol
Year1999
Volume308
Pages111-45
AuthorsAnderson KS
TitleFundamental mechanisms of substrate channeling.
[49]
PubMed ID10386870
JournalProtein Sci
Year1999
Volume8
Pages1200-9
AuthorsZitzewitz JA, Gualfetti PJ, Perkons IA, Wasta SA, Matthews CR
TitleIdentifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein.
[50]
PubMed ID10769125
JournalBiochemistry
Year2000
Volume39
Pages4692-703
AuthorsFan YX, McPhie P, Miles EW
TitleRegulation of tryptophan synthase by temperature, monovalent cations, and an allosteric ligand. Evidence from Arrhenius plots, absorption spectra, and primary kinetic isotope effects.
[51]
CommentsX-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
Medline ID20576265
PubMed ID11034989
JournalJ Biol Chem
Year2000
Volume275
Pages41058-63
AuthorsWeyand M, Schlichting I
TitleStructural basis for the impaired channeling and allosteric inter-subunit communication in the beta A169L/beta C170W mutant of tryptophan synthase.
Related PDB1fuy
Related Swiss-protP00929,P0A2K1
[52]
PubMed ID11412095
JournalBiochemistry
Year2001
Volume40
Pages7421-32
AuthorsFerrari D, Yang LH, Miles EW, Dunn MF
TitleBeta D305A mutant of tryptophan synthase shows strongly perturbed allosteric regulation and substrate specificity.
[53]
CommentsX-ray crystallography
PubMed ID11118452
JournalJ Biol Chem
Year2001
Volume276
Pages11062-71
AuthorsYamagata Y, Ogasahara K, Hioki Y, Lee SJ, Nakagawa A, Nakamura H, Ishida M, Kuramitsu S, Yutani K
TitleEntropic stabilization of the tryptophan synthase alpha-subunit from a hyperthermophile, Pyrococcus furiosus. X-ray analysis and calorimetry.
Related PDB1geq
[54]
PubMed ID12146962
JournalBiochemistry
Year2002
Volume41
Pages9982-90
AuthorsHarris RM, Dunn MF
TitleIntermediate trapping via a conformational switch in the Na(+)-activated tryptophan synthase bienzyme complex.
[55]
PubMed ID12146963
JournalBiochemistry
Year2002
Volume41
Pages9991-10001
AuthorsHur O, Niks D, Casino P, Dunn MF
TitleProton transfers in the beta-reaction catalyzed by tryptophan synthase.
[56]
PubMed ID11756459
JournalJ Biol Chem
Year2002
Volume277
Pages8194-201
AuthorsHettwer S, Sterner R
TitleA novel tryptophan synthase beta-subunit from the hyperthermophile Thermotoga maritima. Quaternary structure, steady-state kinetics, and putative physiological role.
[57]
CommentsX-ray crystallography
PubMed ID11756454
JournalJ Biol Chem
Year2002
Volume277
Pages10653-60
AuthorsWeyand M, Schlichting I, Herde P, Marabotti A, Mozzarelli A
TitleCrystal structure of the beta Ser178--> Pro mutant of tryptophan synthase. A "knock-out" allosteric enzyme.
Related PDB1beu,1k8y,1k8z
[58]
PubMed ID11756456
JournalJ Biol Chem
Year2002
Volume277
Pages10647-52
AuthorsWeyand M, Schlichting I, Marabotti A, Mozzarelli A
TitleCrystal structures of a new class of allosteric effectors complexed to tryptophan synthase.
Related PDB1k3u,1k7e,1k7f
[59]
PubMed ID12460570
JournalJ Mol Biol
Year2002
Volume324
Pages677-90
AuthorsKulik V, Weyand M, Seidel R, Niks D, Arac D, Dunn MF, Schlichting I
TitleOn the role of alphaThr183 in the allosteric regulation and catalytic mechanism of tryptophan synthase.
Related PDB1k8x,1kfb,1kfc,1kfe,1kfj,1kfk

comments
This enzyme catalyzes two separate reactions on different chains. The beta chain has got the type II PLP-dependent enzyme fold, whereas the alpha chain has (alpha/beta)8 barrel fold.
The alpha chain catalyzes the conversion of 1-(indol-3-yl)glycerol 3-phosphate (IGP) to indole and glyceraldehyde 3-phosphate (G3P) (Eq.1). Then, the beta chain catalyzes the conversion of serine (Ser) and indole to tryptophan (Trp)(Eq.2).
Although monovalent cation does not interact directly with substrate or intermediate, it promotes some parts of reactions (see [21], [22], [44], [45] & [50]).
Each reaction can be described in terms of RLCP classification as follows:
(Eq.1) IGP = Indole + G3P (or alpha-reaction)
(A) Eliminative double-bond formation (Elimination of indole leads to carbonyl formation)
(Eq.2) Ser + Indole = Trp + H2O (or beta-reaction; beta-replacement among PLP-dependent reactions)
(B) Exchange of double-bonded atoms; Formation of external aldimine
(C) Isomerization (shift of double-bond position) forming a quinonoid intermediate
(D) Eliminative double-bond formation (Elimination of hydroxyl group from the intermediate) forming an aminoacrylate intermediate
(E) Additive double-bond deformation (Addition of indole to the intermediate) forming a quinonoid intermediate
(F) Isomerization (shift of double-bond position) forming external aldimine
(G) Exchange of double-bonded atoms; Formation of internal aldimine, releasing the product, Trp.
The catalytic reactions proceeds as follows:
(A) Eliminative double-bond formation (Elimination of indole leads to carbonyl formation) (see [29], [38], [42] & [59])
(A1) Thr183 of alpha-chain may act as a modulator for Asp60 by orienting the catalytic residue (see [59]). Asp60 polarize the N-H bond of indole group.
(A2) The first general base, Asp60 of alpha-chain, deprotonates the indole nitrogen, whereas the first general acid protonates the C3 atom of the indole ring (eliminated site of the eliminated group). Here, although the paper [42] suggested that Tyr175 of alpha-chain may play the role as the acid, the other paper [38] reported that Tyr175 is not the essential residue in catalysis, and suggested that Glu49 of alpha-chain may protonate the indole ring. This reaction leads to the tetrahedral transition state at the C3 atom of the indole.
(A3) The second general base, Glu49, deprotonates the C3' hydroxyl group, whilst the second general acid, Asp60, protonates the indole nitrogen atom. This reaction leads to the C3-C3' bond cleavage, and formation of carbonyl group at the C3' atom.
(B) Exchange of double-bonded atoms; Formation of external aldimine (see [17] & [46])
(B1) Asp305 (of beta-chain) may act as a general base to deprotonate the amine group of the incoming substrate, L-serine. The proton must be donated to the sidechain nitrogen of Lys87.
(B2) The activated amine group makes a nucleophilic attack on the C4' atom of PLP, forming a gem-diamine (tetrahedral) intermediate.
(B3) Again, Asp305 may act as a general base to deprotonate the amine group of L-serine, so that the lone pair on the amine group can make a nucleophilic attack on the C4' atom. This reaction leads to the release of Lys87, which is unprotonated for the next reaction.
(C) Isomerization (shift of double-bond position) forming a quinonoid intermediate
(C1) His86 may modulate the activity of Lys87. (Monovalent ion might affect this reaction (see [45]).
(C2) Lys87 may act as a general base to abstract the alpha-proton of Ser-PLP, forming a quinonoid intermediate.
(D) Eliminative double-bond formation (Elimination of hydroxyl group from the intermediate) forming an aminoacrylate intermediate (see [46])
(D1) Asp305 acts as a general acid to protonate the hydroxyl group, leading to the elimination of a water molecule and to the double-bond formation between the alpha- and beta-carbon atoms.
(E) Additive double-bond deformation (Addition of indole to the intermediate) forming a quinonoid intermediate (see [11] & [48])
(E1) Monovalent ion might affect this reaction (see [44]).
(E2) Indole makes a nucleophilic attack on the beta-carbon of the aminoacrylate intermediate.
(E3) A general base must deprotonate the C-3 proton of the indole group. Glu109 may acts as a general base (see [11]).
(F) Isomerization (shift of double-bond position) forming an external aldimine (see [46]).
(F1) His86 may modulate the activity of Lys87.
(F2) Lys87 may act as a general acid to protonate the alpha-carbon of Trp-PLP, leading to the formation of external aldimine.
(G) Exchange of double-bonded atoms; Formation of internal aldimine, releasing the product, Trp. (This reaction is inverse one of external aldimine formation)
(G1) His86 may act as a general base to deprotonate the amine group of Lys87. The proton must be donated to the leaving nitrogen of L-tryptophan (probably by His86). (As Asp305 is located opposite to Lys87, the nearby His86 may act as a base.)
(G2) The activated amine group of Lys87 makes a nucleophilic attack on the C4' atom of PLP, forming a gem-diamine (tetrahedral) intermediate.
(G3) A general base, probably His86, must deprotonate the amine group of Lys87, so that the lone pair on the amine group can make a nucleophilic attack on the C4' atom. This reaction leads to the release of the product, L-tryptophan.

createdupdated
2004-07-022009-04-03
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)

© Computational Biology Research Center, AIST, 2004 All Rights Reserved.