Quinate dehydrogenase (quinone)
Appearance
Quinate dehydrogenase (quinone) | |||||||||
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Identifiers | |||||||||
EC no. | 1.1.5.8 | ||||||||
CAS no. | 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 | ||||||||
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Quinate dehydrogenase (quinone) (EC 1.1.5.8, NAD(P)+-independent quinate dehydrogenase, quinate:pyrroloquinoline-quinone 5-oxidoreductase) is an enzyme with systematic name quinate:quinol 3-oxidoreductase.[1][2][3] This enzyme catalyses the following chemical reaction
This enzyme is membrane-bound.
References
[edit]- ^ van Kleef MA, Duine JA (May 1988). "Bacterial NAD(P)-independent quinate dehydrogenase is a quinoprotein". Archives of Microbiology. 150 (1): 32–6. Bibcode:1988ArMic.150...32V. doi:10.1007/BF00409714. PMID 3044290.
- ^ Adachi O, Tanasupawat S, Yoshihara N, Toyama H, Matsushita K (October 2003). "3-dehydroquinate production by oxidative fermentation and further conversion of 3-dehydroquinate to the intermediates in the shikimate pathway". Bioscience, Biotechnology, and Biochemistry. 67 (10): 2124–31. doi:10.1271/bbb.67.2124. PMID 14586099.
- ^ Vangnai AS, Toyama H, De-Eknamkul W, Yoshihara N, Adachi O, Matsushita K (December 2004). "Quinate oxidation in Gluconobacter oxydans IFO3244: purification and characterization of quinoprotein quinate dehydrogenase". FEMS Microbiology Letters. 241 (2): 157–62. doi:10.1016/j.femsle.2004.10.014. PMID 15598527.
External links
[edit]- Quinate+dehydrogenase+(quinone) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)