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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1nvt

E.C. nameshikimate dehydrogenase
SpeciesMethanococcus jannaschii ()
E.C. Number (IntEnz) 1.1.1.25
CSA Homologues of 1nvtThere are 24 Homologs
CSA Entries With UniProtID Q58484
CSA Entries With EC Number 1.1.1.25
PDBe Entry 1nvt
PDBSum Entry 1nvt
MACiE Entry 1nvt

Literature Report

IntroductionShikimate dehydrogenase catalyses the fourth step of the shikimate pathway, an essential aromatic biosynthesis pathway in plants and microorganisms. This enzyme belongs to the shikimate dehydrogenase family, in the superfamily of NAD(P)H-dependent oxidoreductases.
The shikimate pathway is an attractive target for antifungal, antiparasite and herbicidal agents, and also for research into possible biosynthesis of hydroaromatic compounds for industrial processes.
MechansimShikimate 5-dehydrogenase catalyses the reduction of 3-dehydroshikimate to shikimate using an NADH cofactor. Asp 102 acts as a general acid/base catalyst in the reversible reaction, acting as an acid in the reduction of 3-dehydroshikimate to shikimate by protonation on the C3 hydroxyl in the hydride transfer step by NADH.
Reaction

Catalytic Sites for 1nvt

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AspA10297macie:sideChainParticipates in general acid/base catalysis during hydride transfer.

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AspB10297macie:sideChainParticipates in general acid/base catalysis during hydride transfer.

Literature References

Notes:
Benach J
The 2.3-A crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase.
J Biol Chem 2003 278 19176-19182
PubMed: 12624088
Padyana AK
Crystal structure of shikimate 5-dehydrogenase (SDH) bound to NADP: insights into function and evolution.
Structure 2003 11 1005-1013
PubMed: 12906831
Michel G
Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities.
J Biol Chem 2003 278 19463-19472
PubMed: 12637497
Ye S
The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode.
J Bacteriol 2003 185 4144-4151
PubMed: 12837789
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