3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase explained

[3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] kinase
Ec Number:	2.7.11.4
Cas Number:	82391-38-6
Go Code:	0047323

In enzymology, a [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] is an enzyme that catalyzes the chemical reaction

ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)]

\rightleftharpoons 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]

Literature

• Paxton R, Harris RA . 1982 . Isolation of rabbit liver branched chain alpha-ketoacid dehydrogenase and regulation by phosphorylation . J. Biol. Chem. . 257 . 14433 - 9 . 7142221 . 23 .
• 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 . 30512 - 9 . 10903321 . 10.1074/jbc.M005075200 . 39 . free .
• 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 . 36905 - 8 . 12189132 . 10.1074/jbc.C200430200 . 40 . free .
• Popov KM, Hawes JW, Harris RA . 1997 . Mitochondrial alpha-ketoacid dehydrogenase kinases: a new family of protein kinases . Adv. Second. Messenger. Phosphoprotein. Res. . 31 . 105 - 11 . 9344245 . 10.1016/S1040-7952(97)80012-2 . Advances in Second Messenger and Phosphoprotein Research . 9780120361311 .

Notes and References

1. Novarino . G. . El-Fishawy . P. . Kayserili . H. . Meguid . N. A. . Nagwa Abdel Meguid . 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. . 2012 . Mutations in BCKD-kinase Lead to a Potentially Treatable Form of Autism with Epilepsy . Science . 338 . 6105 . 394–397 . 10.1126/science.1224631 . 3704165 . 22956686 . Matern . D. . Gabriel . S. . Sweetman . L. . Rahimi . Y. . Harris . R. A. . State . M. W. . Gleeson . J. G..