EC number:1.1.1.85
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: | 1.1.1.85 | ||
|---|---|---|---|
| Description: | 3-isopropylmalate dehydrogenase. | ||
| Alternative Name: |
IMDH. Beta-isopropylmalate dehydrogenase. Beta-IPM dehydrogenase. | ||
| Prosite: | PDOC00389; | ||
| PDB: |
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| Cath: | 3.40.718.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.1.1.85 |
| BRENDA Enzyme Link: | BRENDA 1.1.1.85 |
| KEGG Enzyme Link: | KEGG1.1.1.85 |
| BioCyc Enzyme Link: | BioCyc 1.1.1.85 |
| ExPASy Enzyme Link: | ExPASy1.1.1.85 |
| EC2PDB Enzyme Link: | EC2PDB 1.1.1.85 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.1.1.85 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.1.1.85 |
| IntEnz Enzyme Link: | IntEnz 1.1.1.85 |
| MEDLINE Enzyme Link: | MEDLINE 1.1.1.85 |
| RHEA:32271 | (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO2 + NADH |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[OH;+0:3])-[CH;+0:4](-[*:5])-[C;H0;+0:6](=[*:7])-[OH;+0:8].[*: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](=[O;H0;+0:3])-[CH2;+0:4]-[*:5].[*:9]-[N;H0;+0:10]1-[CH;+0:11]=[CH;+0:12]-[CH2;+0:13]-[C;H0;+0:14](-[*:15])=[CH;+0:16]-1.[*:7]=[C;H0;+0:6]=[O;H0;+0:8] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Purification and properties of beta-isopropylmalate dehydrogenase. | Parsons SJ, Burns RO | 1969 Feb 10 | 4889950 |
| THE ABSOLUTE CONFIGURATION OF ALPHA-HYDROXY-BETA-CARBOXYISOCAPROIC ACID (3-ISOPROPYLMALIC ACID), AN INTERMEDIATE IN LEUCINE BIOSYNTHESIS. | CALVO JM, STEVENS CM, KALYANPUR MG, UMBARGER HE | 1964 Dec | 14269331 |
| THE BIOSYNTHESIS OF LEUCINE. III. THE CONVERSION OF ALPHA-HYDROXY-BETA-CARBOXYISOCAPROATE TO ALPHA-KETOISOCAPROATE. | BURNS RO, UMBARGER HE, GROSS SR | 1963 Sep-Oct | 14087358 |
| Mirror image mutations reveal the significance of an intersubunit ion cluster in the stability of 3-isopropylmalate dehydrogenase. | Németh A, Svingor A, Pócsik M, Dobó J, Magyar C, Szilágyi A, Gál P, Závodszky P | 2000 Feb 18 | 10683439 |