Quinate dehydrogenase (pyrroloquinoline-quinone)
| quinate dehydrogenase (pyrroloquinoline-quinone) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.1.99.25 | ||||||||
| CAS number | 115299-99-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
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.
References
- van Kleef MA, Duine JA (1988). "Bacterial NAD(P)-independent quinate dehydrogenase is a quinoprotein". Arch. Microbiol. 150 (1): 32&ndash, 6. doi:10.1007/BF00409714. 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 (10): 2124&ndash, 31. doi:10.1271/bbb.67.2124. PMID 14586099.
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