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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1arz

E.C. namedihydrodipicolinate reductase
SpeciesEscherichia coli (Bacteria)
E.C. Number (IntEnz) 1.3.1.26
CSA Homologues of 1arzThere are 13 Homologs
CSA Entries With UniProtID P04036
CSA Entries With EC Number 1.3.1.26
PDBe Entry 1arz
PDBSum Entry 1arz
MACiE Entry 1arz

Literature Report

IntroductionDihydrodipicolinate reductase catalyzes the NADH-dependent reduction of the α,β-unsaturated cyclic imine dihydrodipicolinate to form the cyclic imine tetrahydrodipicolinate. The enzyme is a component of the biosynthetic pathway that leads to diaminopimelate and lysine in bacteria and higher plants. Because these pathways are unique to microorganisms and plants, they may represent attractive targets for new antimicrobial or herbicidal compounds.
MechansimLysine polarises the imine to promote hydride transfer from NADH, and then stabilises the enemine intermediate. The intermediate then removes a proton from water, which is activated by histidine.
Reaction

Catalytic Sites for 1arz

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
LysA163163macie:sideChainPolarises alpha,beta-unsaturated imine, stabilises enemine intermediate.
HisA159159macie:sideChainActivates a water molecule to protonate the intermediate.

Literature References

Notes:
Scapin G
Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase in complex with NADH and the inhibitor 2,6-pyridinedicarboxylate.
Biochemistry 1997 36 15081-15088
PubMed: 9398235
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