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Catalytic Site Atlas Version 2.2.12
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CSA entry for 1q3n
Original Entry
2-dehydro-3-deoxyphosphooctonate aldolase
EC Class:
Other CSA Entries:
Overview of all sites for 1q3n
Homologues of 1q3n
Entries for UniProt/Swiss-Prot: P17579
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PDB entry: 1q3n
PDBsum entry: 1q3n
UniProt/Swiss-Prot: P17579
IntEnz entry:
Literature Report:
3-deoxy-d-manno-s-octulosonate-8-phosphate synthase from E.coli (KDOPS) is responsible for the synthesis of the named product from Phosphenol Pyruvate (PEP) and arabinose-5-phosphate (A5P). It thus plays a role in the synthesis of complex lipids for the gram negative bacterial cell wall, so is a possible target for antibiotics. It displays homology with many PEP utilising enzymes, particularly the metal dependent enzyme DAHP synthase which works by a similar mechanism.
The reaction proceeds in a stepwise manner with initial attack from the C3 nucleophile of PEP attacking the reducing end of A5P. This forms a carbocation intermediate which is attacked by a water molecule, activated by His 202, to form a second linear intermediate which undergoes cyclisation to form the product.

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Found by:
Literature reference 

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
HISA 202 202Sidechain
Activates a water molecule which can act as a nucleophile to attack the carbocation intermediate formed by the initial condensation of A5P and PEP.
Evidence from paper Evidence concerns Evidence type
PubMed ID 10734095 Current protein Residue is positioned appropriately (ligand position known)
PubMed ID 10734095 Current protein Mutagenesis of residue
Structure and mechanism of 3-deoxy-D-manno-octulosonate 8-phosphate synthase.
S. Radaev and P. Dastidar and M. Patel and R. W. Woodard and D. L. Gatti
J Biol Chem 275, (13) 9476-84, (2000).
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