EzCatDB: S00201

DB codeS00201
CATH domainDomain 13.20.20.70Catalytic domain
E.C.4.2.1.52
CSA1dhp
MACiEM0267

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,S00221,S00222,S00847,S00224,S00225,S00226,D00014,D00029,M00141,T00015,T00239,D00664,D00665,D00804,D00863,T00089

Enzyme Name
Swiss-protKEGG

P0A6L2
Protein nameDihydrodipicolinate synthasedihydrodipicolinate synthase
dihydropicolinate synthetase
dihydrodipicolinic acid synthase
L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate andcyclizing)
SynonymsDHDPS
EC 4.2.1.52

KEGG pathways
MAP codePathways
MAP00300Lysine biosynthesis

Swiss-prot:Accession NumberP0A6L2
Entry nameDAPA_ECOLI
ActivityL-aspartate 4-semialdehyde + pyruvate = dihydrodipicolinate + 2 H(2)O.
SubunitHomotetramer.
Subcellular locationCytoplasm.
Cofactor


CofactorsSubstratesProducts
KEGG-idC00238C00441C00022C03340C00001
CompoundPotassiumL-Aspartate 4-semialdehydePyruvate2,3-DihydrodipicolinateH2O
Typeunivalent metal (Na+, K+)amino acids,carbohydratecarbohydrate,carboxyl grouparomatic ring (with nitrogen atoms),carboxyl groupH2O
1dhpABound:__KUnboundUnboundUnbound
1dhpBBound:__KUnboundUnboundUnbound

Active-site residues
resource
PDB;1dhp & Swiss-prot;P0A6L2
pdbCatalytic residues
1dhpALYS 161;TYR 133
1dhpBLYS 161;TYR 133

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]Fig.1, p.2316
[3]Fig.7, p.30-325
[4]Scheme 5, p.17398
[5]Fig.15
[6]Fig.13

references
[1]
PubMed ID1463470
JournalBiochem J
Year1992
Volume288
Pages691-5
AuthorsLaber B, Gomis-Ruth FX, Romao MJ, Huber R
TitleEscherichia coli dihydrodipicolinate synthase. Identification of the active site and crystallization.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Medline ID95156485
PubMed ID7853400
JournalJ Mol Biol
Year1995
Volume246
Pages227-39
AuthorsMirwaldt C, Korndorfer I, Huber R
TitleThe crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution.
Related PDB1dhp
Related Swiss-protP0A6L2
[3]
CommentsX-RAY CRYSTALLOGRAPHY, AND CATALYTIC MECHANISM.
Medline ID97146458
PubMed ID8993314
JournalBiochemistry
Year1997
Volume36
Pages24-33
AuthorsBlickling S, Renner C, Laber B, Pohlenz HD, Holak TA, Huber R
TitleReaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by X-ray crystallography and NMR spectroscopy.
Related Swiss-protP0A6L2
[4]
PubMed ID9048556
JournalBiochemistry
Year1997
Volume36
Pages1730-9
AuthorsKarsten WE
TitleDihydrodipicolinate synthase from Escherichia coli: pH dependent changes in the kinetic mechanism and kinetic mechanism of allosteric inhibition by L-lysine.
[5]
PubMed ID9417939
JournalJ Mol Biol
Year1997
Volume274
Pages608-21
AuthorsBlickling S, Beisel HG, Bozic D, Knablein J, Laber B, Huber R
TitleStructure of dihydrodipicolinate synthase of Nicotiana sylvestris reveals novel quaternary structure.
[6]
PubMed ID9047371
JournalJ Mol Biol
Year1997
Volume266
Pages381-99
AuthorsLawrence MC, Barbosa JA, Smith BJ, Hall NE, Pilling PA, Ooi HC, Marcuccio SM
TitleStructure and mechanism of a sub-family of enzymes related to N-acetylneuraminate lyase.
[7]
PubMed ID12711733
JournalProc Natl Acad Sci U S A
Year2003
Volume100
Pages5694-9
AuthorsJoerger AC, Mayer S, Fersht AR
TitleMimicking natural evolution in vitro: an N-acetylneuraminate lyase mutant with an increased dihydrodipicolinate synthase activity.


createdupdated
2004-06-282009-03-19


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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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