EC number:1.1.5.8

Enzyme

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     1. Oxidoreductases
        1.1 Acting on the CH-OH group of donors
            1.1.5 With a quinone or similar compound as acceptor
ID:1.1.5.8
Description:Quinate dehydrogenase (quinone).
Alternative Name: NAD(P)(+)-independent quinate dehydrogenase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.1.5.8
BRENDA Enzyme Link: BRENDA 1.1.5.8
KEGG Enzyme Link: KEGG1.1.5.8
BioCyc Enzyme Link: BioCyc 1.1.5.8
ExPASy Enzyme Link: ExPASy1.1.5.8
EC2PDB Enzyme Link: EC2PDB 1.1.5.8
ExplorEnz Enzyme Link: ExplorEnz 1.1.5.8
PRIAM enzyme-specific profiles Link: PRIAM 1.1.5.8
IntEnz Enzyme Link: IntEnz 1.1.5.8
MEDLINE Enzyme Link: MEDLINE 1.1.5.8

EC number:1.1.5.8

MSA:

1.1.5.8;
Phylogenetic Tree:

1.1.5.8;
Uniprot:
M-CSA:
RHEA:23672 a quinone + L-quinate = 3-dehydroquinate + a quinol
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[OH;+0:4].[O;H0;+0:5]=[C;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[C;H0;+0:9](=[O;H0;+0:10])-[CH;+0:11]=[CH;+0:12]-1>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[OH;+0:5]-[c;H0;+0:6]1:[cH;+0:7]:[cH;+0:8]:[c;H0;+0:9](-[OH;+0:10]):[cH;+0:11]:[cH;+0:12]:1
Reaction
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References

TitleAuthorsDatePubMed ID
Bacterial NAD(P)-independent quinate dehydrogenase is a quinoprotein.van Kleef MA, Duine JA1988 May3044290
Quinate oxidation in Gluconobacter oxydans IFO3244: purification and characterization of quinoprotein quinate dehydrogenase.Vangnai AS, Toyama H, De-Eknamkul W, Yoshihara N, Adachi O, Matsushita K2004 Dec 1515598527
3-dehydroquinate production by oxidative fermentation and further conversion of 3-dehydroquinate to the intermediates in the shikimate pathway.Adachi O, Tanasupawat S, Yoshihara N, Toyama H, Matsushita K2003 Oct14586099