EC number:1.1.1.282
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.1 Acting on the CH-OH group of donors |
| 1.1.1 With NAD+ or NADP+ as acceptor |
| ID: | 1.1.1.282 |
|---|---|
| Description: | Quinate/shikimate dehydrogenase. |
| Alternative Name: |
Quinic dehydrogenase. Quinate dehydrogenase. |
| Cath: | 3.40.50.720; 3.40.50.10860; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.1.1.282 |
| BRENDA Enzyme Link: | BRENDA 1.1.1.282 |
| KEGG Enzyme Link: | KEGG1.1.1.282 |
| BioCyc Enzyme Link: | BioCyc 1.1.1.282 |
| ExPASy Enzyme Link: | ExPASy1.1.1.282 |
| EC2PDB Enzyme Link: | EC2PDB 1.1.1.282 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.1.1.282 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.1.1.282 |
| IntEnz Enzyme Link: | IntEnz 1.1.1.282 |
| MEDLINE Enzyme Link: | MEDLINE 1.1.1.282 |
EC number:1.1.1.282
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:17737 | NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH |
| 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 |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The conserved Lysine69 residue plays a catalytic role in Mycobacterium tuberculosis shikimate dehydrogenase. | Rodrigues VS Jr, Breda A, Santos DS, Basso LA | 2009 Nov 16 | 19917104 |
| Structural and biochemical analyses of shikimate dehydrogenase AroE from Aquifex aeolicus: implications for the catalytic mechanism. | Gan J, Wu Y, Prabakaran P, Gu Y, Li Y, Andrykovitch M, Liu H, Gong Y, Yan H, Ji X | 2007 Aug 21 | 17649975 |
| Kinetic and chemical mechanisms of shikimate dehydrogenase from Mycobacterium tuberculosis. | Fonseca IO, Silva RG, Fernandes CL, de Souza ON, Basso LA, Santos DS | 2007 Jan 15 | 17178095 |
| Structure of Arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase and implications for metabolic channeling in the shikimate pathway. | Singh SA, Christendat D | 2006 Jun 27 | 16784230 |
| Crystal structure of a novel shikimate dehydrogenase from Haemophilus influenzae. | Singh S, Korolev S, Koroleva O, Zarembinski T, Collart F, Joachimiak A, Christendat D | 2005 Apr 29 | 15735308 |
| 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 |
| The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode. | Ye S, Von Delft F, Brooun A, Knuth MW, Swanson RV, McRee DE | 2003 Jul | 12837789 |
| 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 |
| The 2.3-A crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase. | Benach J, Lee I, Edstrom W, Kuzin AP, Chiang Y, Acton TB, Montelione GT, Hunt JF | 2003 May 23 | 12624088 |
| RHEA:17741 | NAD(+) + shikimate = 3-dehydroshikimate + 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 |
References
| Title | Authors | Date | PubMed 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 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 |
| The 2.3-A crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase. | Benach J, Lee I, Edstrom W, Kuzin AP, Chiang Y, Acton TB, Montelione GT, Hunt JF | 2003 May 23 | 12624088 |
| RHEA:18425 | L-quinate + NADP(+) = 3-dehydroquinate + H(+) + NADPH |
| 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 |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| 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 |
| 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 |
References
| Title | Authors | Date | PubMed 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 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 |