3-dehydroquinate synthase

From Wikipedia, the free encyclopedia

In enzymology, a 3-dehydroquinate synthase (EC 4.2.3.4) is an enzyme that catalyzes the chemical reaction

3-deoxy-arabino-heptulonate 7-phosphate $\rightleftharpoons$ 3-dehydroquinate + phosphate

Hence, this enzyme has one substrate, 3-deoxy-arabino-heptulonate 7-phosphate, and two products, 3-dehydroquinate and phosphate.

This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is 3-deoxy-arabino-heptulonate-7-phosphate phosphate-lyase (cyclizing 3-dehydroquinate-forming). Other names in common use include 5-dehydroquinate synthase, 5-dehydroquinic acid synthetase, dehydroquinate synthase, 3-dehydroquinate synthetase, 3-deoxy-arabino-heptulosonate-7-phosphate phosphate-lyase, (cyclizing), and 3-deoxy-arabino-heptulonate-7-phosphate phosphate-lyase (cyclizing). This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis. It employs one cofactor, cobalt.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 15 structures have been solved for this class of enzymes, with PDB accession codes 1NR5, 1NRX, 1NUA, 1NVA, 1NVB, 1NVD, 1NVE, 1NVF, 1SG6, 1UJN, 1XAG, 1XAH, 1XAI, 1XAJ, and 1XAL.

[edit] References

IUBMB entry for 4.2.3.4
BRENDA references for 4.2.3.4 (Recommended.)
PubMed references for 4.2.3.4
PubMed Central references for 4.2.3.4
Google Scholar references for 4.2.3.4
Rotenberg SL, Sprinson DB (1970). "Mechanism and stereochemistry of 5-dehydroquinate synthetase". Proc. Natl. Acad. Sci. U. S. A. 67: 1669–72. doi:10.1073/pnas.67.4.1669. PMID 5275368.
SRINIVASAN PR, ROTHSCHILD J, SPRINSON DB (1963). "THE ENZYMIC CONVERSION OF 3-DEOXY-D-ARABINO-HEPTULOSONIC ACID 7-PHOSPHATE TO 5-DEHYDROQUINATE". J. Biol. Chem. 238: 3176–82. PMID 14085358.
Bender SL, Mehdi S, Knowles JR (1989). "Dehydroquinate synthase: the role of divalent metal cations and of nicotinamide adenine dinucleotide in catalysis". Biochemistry. 28: 7555–60. doi:10.1021/bi00445a009. PMID 2514789.
Carpenter EP, Hawkins AR, Frost JW, Brown KA (1998). "Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis". Nature. 394: 299–302. doi:10.1038/28431. PMID 9685163.