| [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.
Well, that’s interesting to know that Psilotum nudum are known as whisk ferns. Psilotum nudum is the commoner species of the two. While the P. flaccidum is a rare species and is found in the tropical islands. Both the species are usually epiphytic in habit and grow upon tree ferns. These species may also be terrestrial and grow in humus or in the crevices of the rocks.
View the detailed Guide of Psilotum nudum: Detailed Study Of Psilotum Nudum (Whisk Fern), Classification, Anatomy, Reproduction