| EC Tree |
| 1. Oxidoreductases |
| 1.2 Acting on the aldehyde or oxo group of donors |
| 1.2.4 With a disulfide as acceptor |
| ID: | 1.2.4.4 |
|---|---|
| Description: | 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring). |
| Alternative Name: |
Dehydrogenase, branched chain alpha-keto acid. Dehydrogenase, 2-oxoisovalerate (lipoate). Branched-chain ketoacid dehydrogenase. Branched-chain keto acid dehydrogenase. Branched-chain alpha-oxo acid dehydrogenase. Branched-chain alpha-keto acid dehydrogenase. Branched-chain 2-oxo acid dehydrogenase. Branched-chain 2-keto acid dehydrogenase. Branched-chain (-2-oxoacid) dehydrogenase (BCD). Branched chain keto acid dehydrogenase. BCOAD. BCKDH. Alpha-oxoisocaproate dehydrogenase. Alpha-ketoisovalerate dehydrogenase. Alpha-ketoisocaproic-alpha-keto-alpha-methylvaleric dehydrogenase. Alpha-ketoisocaproic dehydrogenase. Alpha-ketoisocaproate dehydrogenase. Alpha-keto-alpha-methylvalerate dehydrogenase. acceptor-2-methylpropanoylating). 3-methyl-2-oxobutanoate:lipoamide oxidoreductase (decarboxylating and 3-methyl-2-oxobutanoate dehydrogenase (lipoamide). 2-oxoisovalerate (lipoate) dehydrogenase. 2-oxoisocaproate dehydrogenase. |
| Cath: | 1.20.140.20; 3.30.559.10; 3.30.565.10; 4.10.320.10; 3.40.50.920; 3.40.50.970; 2.40.50.100; |
Click one PDB to see exact 3D structure provided by NGL.
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 1.2.4.4 |
| BRENDA Enzyme Link: | BRENDA 1.2.4.4 |
| KEGG Enzyme Link: | KEGG1.2.4.4 |
| BioCyc Enzyme Link: | BioCyc 1.2.4.4 |
| ExPASy Enzyme Link: | ExPASy1.2.4.4 |
| EC2PDB Enzyme Link: | EC2PDB 1.2.4.4 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.2.4.4 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.2.4.4 |
| IntEnz Enzyme Link: | IntEnz 1.2.4.4 |
| MEDLINE Enzyme Link: | MEDLINE 1.2.4.4 |
| RHEA:13457 | 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]-(R)-N(6)-lipoyl-L-lysine + H(+) = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]-(R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysine + CO2 |
| RULE(radius=1) | [*:1]-[S;H0;+0:2]-[S;H0;+0:3]-[*:4].[*:5]=[C;H0;+0:6](-[OH;+0:7])-[C;H0;+0:8](=[*:9])-[*:10].[H+;H0:11]>>([*:4]-[S;H0;+0:3]-[C;H0;+0:8](=[*:9])-[*:10].[*:1]-[SH;+0:2]).[*:5]=[C;H0;+0:6]=[O;H0;+0:7] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Branched chain alpha-keto acid metabolism. I. Isolation, purification, and partial characterization of bovine liver alpha-ketoisocaproic:alpha-keto-beta-methylvaleric acid dehydrogenase. | Connelly JL, Danner DJ, Bowden JA | 1968 Mar 25 | 5689906 |
| Branched chain alpha-keto acid metabolism. II. Evidence for the common identity of alpha-ketoisocaproic acid and alpha-keto-beta-methyl-valeric acid dehydrogenases. | Bowden JA, Connelly JL | 1968 Jun 25 | 5656388 |
| Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. | Perham RN | 2000 | 10966480 |