3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase
| [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.11.4 | ||||||||
| CAS no. | 82391-38-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] (EC 2.7.11.4) is an enzyme that catalyzes the chemical reaction
- ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate
Thus, the two substrates of this enzyme are ATP and 3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring), whereas its 3 products are ADP, 3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring), and phosphate.
This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases). The systematic name of this enzyme class is ATP:[3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphotransferase. Other names in common use include kinase, BCK, BCKD kinase, BCODH kinase, branched-chain alpha-ketoacid dehydrogenase kinase, branched-chain 2-oxo acid dehydrogenase kinase, branched-chain keto acid dehydrogenase kinase, branched-chain oxo acid dehydrogenase kinase (phosphorylating), and STK2.
In 2012, it was suggested that mutations in the gene which expresses this enzyme could be the cause of a rare form of autism.[1]
References
[edit]- ^ Novarino, G.; El-Fishawy, P.; Kayserili, H.; Meguid, N. A.; Scott, E. M.; Schroth, J.; Silhavy, J. L.; Kara, M.; Khalil, R. O.; Ben-Omran, T.; Ercan-Sencicek, A. G.; Hashish, A. F.; Sanders, S. J.; Gupta, A. R.; Hashem, H. S.; Matern, D.; Gabriel, S.; Sweetman, L.; Rahimi, Y.; Harris, R. A.; State, M. W.; Gleeson, J. G. (2012). "Mutations in BCKD-kinase Lead to a Potentially Treatable Form of Autism with Epilepsy". Science. 338 (6105): 394–397. doi:10.1126/science.1224631. PMC 3704165. PMID 22956686.
Literature
[edit]- Paxton R, Harris RA (1982). "Isolation of rabbit liver branched chain alpha-ketoacid dehydrogenase and regulation by phosphorylation". J. Biol. Chem. 257 (23): 14433–9. PMID 7142221.
- Wynn RM, Chuang JL, Cote CD, Chuang DT (2000). "Tetrameric assembly and conservation in the ATP-binding domain of rat branched-chain alpha-ketoacid dehydrogenase kinase". J. Biol. Chem. 275 (39): 30512–9. doi:10.1074/jbc.M005075200. PMID 10903321.
- Chuang JL, Wynn RM, Chuang DT (2002). "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". J. Biol. Chem. 277 (40): 36905–8. doi:10.1074/jbc.C200430200. PMID 12189132.
- Popov KM, Hawes JW, Harris RA (1997). "Mitochondrial alpha-ketoacid dehydrogenase kinases: a new family of protein kinases". Adv. Second. Messenger. Phosphoprotein. Res. Advances in Second Messenger and Phosphoprotein Research. 31: 105–11. doi:10.1016/S1040-7952(97)80012-2. ISBN 9780120361311. PMID 9344245.
