EC Tree |
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 |
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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; |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.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 |
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 | ![]() |
Core-to-Core | |
Core-to-Core |
Title | Authors | Date | PubMed ID |
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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 K | 2013 Nov | 23929881 |
1.6 angstroms structure of an NAD+-dependent quinate dehydrogenase from Corynebacterium glutamicum. | Schoepe J, Niefind K, Schomburg D | 2008 Jul | 18566515 |
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 M | 2005 Feb 25 | 15596430 |
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 AJ | 2003 May 23 | 12637497 |