Quinate dehydrogenase (pyrroloquinoline-quinone)
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In enzymology, a quinate dehydrogenase (pyrroloquinoline-quinone) (EC 1.1.99.25) is an enzyme that catalyzes the chemical reaction
- quinate + pyrroloquinoline-quinone 3-dehydroquinate + reduced pyrroloquinoline-quinone
Thus, the two substrates of this enzyme are quinate and pyrroloquinoline-quinone, whereas its two products are 3-dehydroquinate and reduced pyrroloquinoline-quinone.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is quinate:pyrroloquinoline-quinone 3-oxidoreductase. Other names in common use include NAD(P)+-independent quinate dehydrogenase, and quinate:pyrroloquinoline-quinone 5-oxidoreductase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis.
[edit] References
- IUBMB entry for 1.1.99.25
- BRENDA references for 1.1.99.25 (Recommended.)
- PubMed references for 1.1.99.25
- PubMed Central references for 1.1.99.25
- Google Scholar references for 1.1.99.25
- van Kleef MA, Duine JA (1988). "Bacterial NAD(P)-independent quinate dehydrogenase is a quinoprotein". Arch. Microbiol. 150: 32–6. doi: . PMID 3044290.
- Adachi O, Tanasupawat S, Yoshihara N, Toyama H, Matsushita K (2003). "3-dehydroquinate production by oxidative fermentation and further conversion of 3-dehydroquinate to the intermediates in the shikimate pathway". Biosci. Biotechnol. Biochem. 67: 2124–31. doi: . PMID 14586099.
[edit] External links
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- The CAS registry number for this enzyme class is 115299-99-5.