| EC Tree |
| 2. Transferases |
| 2.7 Transferring phosphorus-containing groups |
| 2.7.11 Protein-serine/threonine kinases |
| ID: | 2.7.11.4 | ||
|---|---|---|---|
| Description: | [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase. | ||
| Alternative Name: |
Branched-chain oxo acid dehydrogenase kinase (phosphorylating). Branched-chain keto acid dehydrogenase kinase. Branched-chain alpha-ketoacid dehydrogenase kinase. Branched-chain 2-oxo acid dehydrogenase kinase. BCODH kinase. BCKD kinase. BCK. | ||
| Prosite: | PDOC50109; | ||
| PDB: |
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| Cath: | 1.20.140.20; 3.30.565.10; |
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 2.7.11.4 |
| BRENDA Enzyme Link: | BRENDA 2.7.11.4 |
| KEGG Enzyme Link: | KEGG2.7.11.4 |
| BioCyc Enzyme Link: | BioCyc 2.7.11.4 |
| ExPASy Enzyme Link: | ExPASy2.7.11.4 |
| EC2PDB Enzyme Link: | EC2PDB 2.7.11.4 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.7.11.4 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.7.11.4 |
| IntEnz Enzyme Link: | IntEnz 2.7.11.4 |
| MEDLINE Enzyme Link: | MEDLINE 2.7.11.4 |
| RHEA:17301 | [3-methyl-2-oxobutanoate dehydrogenase]-L-serine + ATP = [3-methyl-2-oxobutanoate dehydrogenase]-O-phospho-L-serine + ADP + H(+) |
| RULE(radius=1) | [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:8]-[OH;+0:7].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:2]-[*:1] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Mitochondrial alpha-ketoacid dehydrogenase kinases: a new family of protein kinases. | Popov KM, Hawes JW, Harris RA | 1997 | 9344245 |
| Isolation of rabbit liver branched chain alpha-ketoacid dehydrogenase and regulation by phosphorylation. | Paxton R, Harris RA | 1982 Dec 10 | 7142221 |
| The C-terminal hinge region of lipoic acid-bearing domain of E2b is essential for domain interaction with branched-chain alpha-keto acid dehydrogenase kinase. | Chuang JL, Wynn RM, Chuang DT | 2002 Oct 4 | 12189132 |
| Tetrameric assembly and conservation in the ATP-binding domain of rat branched-chain alpha-ketoacid dehydrogenase kinase. | Wynn RM, Chuang JL, Cote CD, Chuang DT | 2000 Sep 29 | 10903321 |