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Catalytic Site Atlas

CSA LITERATURE entry for 1dqs

E.C. name3-dehydroquinate synthase
SpeciesEmericella nidulans (Fungus)
E.C. Number (IntEnz)
CSA Homologues of 1dqsThere are 36 Homologs
CSA Entries With UniProtID P07547
CSA Entries With EC Number
PDBe Entry 1dqs
PDBSum Entry 1dqs
MACiE Entry M0059

Literature Report

IntroductionDehydroquinate synthase (DHQS) has long been regarded as a catalytic wonder due to its ability to perform several consecutive chemical reactions in one active site. DHQS performs the second step in the shikimate pathway, which is required for the synthesis of aromatic compounds in bacteria, microbial eukaryotes and plants. The fold of the C-terminal domain of DHQS shows no detectable structural relationships to known structures. The active site is located between the two domains. The C-terminal domain contains most of the residues involved in catalysis and in substrate and Zn(2+) binding. The crystal structure of DHQS shows an active site which possesses a variety of interactions between metal, dinucleotide, substrate analogue and protein.
MechansimGeneral base catalysis is prompted by His275, which activates the water molecule (Wat7) to lose its hydrogen. A second general base catalysis is activated by an unknown base, possibly Arg260, accepting a proton from Wat20 and this is then stabilised by Asn268. Lys152 then stabilises the open ring, which reforms after a rotation about the C5-C6 bond and an intramolecular aldol condensation.

Catalytic Sites for 1dqs

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription

Literature References

Carpenter EP
Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis.
Nature 1998 394 299-302
PubMed: 9685163