EC number:1.1.1.86
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: | 1.1.1.86 |
|---|---|
| Description: | Ketol-acid reductoisomerase (NADP(+)). |
| Alternative Name: |
Dihydroxyisovalerate dehydrogenase (isomerizing). Alpha-keto-beta-hydroxylacyl reductoisomerase. Acetohydroxy acid isomeroreductase. |
| Cath: | 1.10.1040.10; 1.10.3730.40; 3.40.50.720; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.1.1.86 |
| BRENDA Enzyme Link: | BRENDA 1.1.1.86 |
| KEGG Enzyme Link: | KEGG1.1.1.86 |
| BioCyc Enzyme Link: | BioCyc 1.1.1.86 |
| ExPASy Enzyme Link: | ExPASy1.1.1.86 |
| EC2PDB Enzyme Link: | EC2PDB 1.1.1.86 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.1.1.86 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.1.1.86 |
| IntEnz Enzyme Link: | IntEnz 1.1.1.86 |
| MEDLINE Enzyme Link: | MEDLINE 1.1.1.86 |
| RHEA:22068 | (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + H(+) + NADPH |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[C;H0;+0:4](-[*:5])(-[CH3;+0:6])-[OH;+0:7].[*:8]-[n+;H0:9]1:[cH;+0:10]:[cH;+0:11]:[cH;+0:12]:[c;H0;+0:13](-[*:14]):[cH;+0:15]:1>>[*:1]-[C;H0;+0:2](-[*:3])(-[CH3;+0:6])-[C;H0;+0:4](-[*:5])=[O;H0;+0:7].[*:8]-[N;H0;+0:9]1-[CH;+0:10]=[CH;+0:11]-[CH2;+0:12]-[C;H0;+0:13](-[*:14])=[CH;+0:15]-1 |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Biosynthesis of valine and isoleucine in plants. 3. Reductoisomerase of Phaseolus radiatus. | Satyanarayana T, Radhakrishnan AN | 1965 Nov 22 | 5866387 |
| Purification and properties of the acetohydroxy acid isomeroreductase of Salmonella typhimurium. | Arfin SM, Umbarger HE | 1969 Mar 10 | 4388025 |
| Artificial domain duplication replicates evolutionary history of ketol-acid reductoisomerases. | Cahn JK, Brinkmann-Chen S, Buller AR, Arnold FH | 2016 Jul | 26644020 |
| Uncovering rare NADH-preferring ketol-acid reductoisomerases. | Brinkmann-Chen S, Cahn JKB, Arnold FH | 2014 Nov | 25172159 |
| Conformational changes in a plant ketol-acid reductoisomerase upon Mg(2+) and NADPH binding as revealed by two crystal structures. | Leung EW, Guddat LW | 2009 May 29 | 19362563 |
| Synthesis, bioactivity and SAR study of N'-(5-substituted-1,3,4-thiadiazol-2-yl)-N-cyclopropylformyl-thioureas as ketol-acid reductoisomerase inhibitors. | Liu XH, Zhang CY, Guo WC, Li YH, Chen PQ, Wang T, Dong WL, Wang BL, Sun HW, Li ZM | 2009 Apr | 18763167 |
| The crystal structure of a bacterial class II ketol-acid reductoisomerase: domain conservation and evolution. | Tyagi R, Duquerroy S, Navaza J, Guddat LW, Duggleby RG | 2005 Dec | 16322583 |
| Probing the mechanism of the bifunctional enzyme ketol-acid reductoisomerase by site-directed mutagenesis of the active site. | Tyagi R, Lee YT, Guddat LW, Duggleby RG | 2005 Jan | 15654896 |
| RHEA:13493 | (2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[C;H0;+0:4](-[*:5])(-[OH;+0:6])-[CH2;+0:7]-[*:8].[*:9]-[n+;H0:10]1:[cH;+0:11]:[cH;+0:12]:[cH;+0:13]:[c;H0;+0:14](-[*:15]):[cH;+0:16]:1>>[*:1]-[C;H0;+0:2](-[*:3])(-[CH2;+0:7]-[*:8])-[C;H0;+0:4](-[*:5])=[O;H0;+0:6].[*:9]-[N;H0;+0:10]1-[CH;+0:11]=[CH;+0:12]-[CH2;+0:13]-[C;H0;+0:14](-[*:15])=[CH;+0:16]-1 |
| Reaction |  |
| Core-to-Core |