The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

Accepted name: 3-dehydroquinate synthase
Reaction: 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate
For diagram of shikimate and chorismate biosynthesis, click here and for mechanism of reaction, click here
Glossary: quinate = (1R,3R,4R,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid and is a cyclitol carboxylate
The numbering system used for the 3-dehydroquinate is that of the recommendations on cyclitols, sections I-8 and I-9: and is shown in the reaction diagram). The use of the term ’5-dehydroquinate’ for this compound is based on an earlier system of numbering.
Other name(s): 5-dehydroquinate synthase; 5-dehydroquinic acid synthetase; dehydroquinate synthase; 3-dehydroquinate synthetase; 3-deoxy-arabino-heptulosonate-7-phosphate phosphate-lyase (cyclizing); 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)
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: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37211-77-1
1.  Rotenberg, S.L. and Sprinson, D.B. Mechanism and stereochemistry of 5-dehydroquinate synthetase. Proc. Natl. Acad. Sci. USA 67 (1970) 1669–1672. [DOI] [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 (1963) 3176–3182. [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 (1989) 7555–7560. [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 (1998) 299–302. [DOI] [PMID: 9685163]
[EC created 1978 as EC, transferred 2000 to EC, modified 2002]

Data © 2001–2022 IUBMB
Web site © 2005–2022 Andrew McDonald