EC 4.2.3.4 - 3-dehydroquinate synthase

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IntEnz Enzyme Nomenclature
EC 4.2.3.4

Names

Accepted name:
3-dehydroquinate synthase
Other names:
3-dehydroquinate synthetase
3-deoxy-arabino-heptulosonate-7-phosphate phosphate-lyase (cyclizing)
5-dehydroquinate synthase
5-dehydroquinic acid synthetase
dehydroquinate synthase
3-deoxy-arabino-heptulonate-7-phosphate phosphate-lyase (cyclizing)
3-deoxy-arabino-heptulonate-7-phosphate phosphate-lyase (cyclizing; 3-dehydroquinate-forming)
Systematic name:
3-deoxy-D-arabino-hept-2-ulosonate-7-phosphate phosphate-lyase (cyclizing; 3-dehydroquinate-forming)

Reaction

Cofactors

Comments:

Requires Co2+ and bound NAD+. The hydrogen atoms on C-7 of the substrate are retained on C-2 of the product.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0003856
CAS Registry Number: 37211-77-1
UniProtKB/Swiss-Prot: (589) [show] [UniProt]

References

  1. Rotenberg, S.L. and Sprinson, D.B.
    Mechanism and stereochemistry of 5-dehydroquinate synthetase.
    Proc. Natl. Acad. Sci. USA 67: 1669-1672 (1970). [PMID: 5275368]
  2. Srinivasan, P.R., Rothschild, J. and Sprinson, D.B.
    The enzymic conversion of 3-deoxy-D-arabino-heptulosonic acid 7-phosphate to 5-dehydroquinate.
    J. Biol. Chem. 238: 3176-3182 (1963). [PMID: 14085358]
  3. Bender, S.L., Mehdi, S. and Knowles, J.R.
    Dehydroquinate synthase: the role of divalent metal cations and of nicotinamide adenine dinucleotide in catalysis.
    Biochemistry 28: 7555-7560 (1989). [PMID: 2514789]
  4. Carpenter, E.P., Hawkins, A.R., Frost, J.W. and Brown, K.A.
    Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis.
    Nature 394: 299-302 (1998). [PMID: 9685163]

[EC 4.2.3.4 created 1978 as EC 4.6.1.3, transferred 2000 to EC 4.2.3.4, modified 2002]