Enzyme

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     1. Oxidoreductases
        1.1 Acting on the CH-OH group of donors
            1.1.1 With NAD+ or NADP+ as acceptor
ID:1.1.1.24
Description:Quinate dehydrogenase.
Alternative Name: Quinic dehydrogenase.
Quinate:NAD(+) 5-oxidoreductase.
Quinate:NAD oxidoreductase.
Quinate 5-dehydrogenase.
Cath: 3.40.50.720; 3.40.50.10860;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.1.1.24
BRENDA Enzyme Link: BRENDA 1.1.1.24
KEGG Enzyme Link: KEGG1.1.1.24
BioCyc Enzyme Link: BioCyc 1.1.1.24
ExPASy Enzyme Link: ExPASy1.1.1.24
EC2PDB Enzyme Link: EC2PDB 1.1.1.24
ExplorEnz Enzyme Link: ExplorEnz 1.1.1.24
PRIAM enzyme-specific profiles Link: PRIAM 1.1.1.24
IntEnz Enzyme Link: IntEnz 1.1.1.24
MEDLINE Enzyme Link: MEDLINE 1.1.1.24
MSA:

1.1.1.24;

Phylogenetic Tree:

1.1.1.24;

Uniprot:
M-CSA:
RHEA:22364 L-quinate + NAD(+) = 3-dehydroquinate + H(+) + NADH
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[OH;+0:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1
Reaction
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References

TitleAuthorsDatePubMed ID
Enzyme-substrate complexes of the quinate/shikimate dehydrogenase from Corynebacterium glutamicum enable new insights in substrate and cofactor binding, specificity, and discrimination.Höppner A, Schomburg D, Niefind K2013 Nov23929881
1.6 angstroms structure of an NAD+-dependent quinate dehydrogenase from Corynebacterium glutamicum.Schoepe J, Niefind K, Schomburg D2008 Jul18566515
Site-directed mutagenesis of the active site region in the quinate/shikimate 5-dehydrogenase YdiB of Escherichia coli.Lindner HA, Nadeau G, Matte A, Michel G, Ménard R, Cygler M2005 Feb 2515596430
Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities.Michel G, Roszak AW, Sauvé V, Maclean J, Matte A, Coggins JR, Cygler M, Lapthorn AJ2003 May 2312637497