“3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase”的意思、由来-开放百科全书

In enzymology, a [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] ({{EC number|2.7.11.4}}) is an enzyme that catalyzes the chemical reaction

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

1. ^{{Cite journal | last1 = Novarino | first1 = G. | last2 = El-Fishawy | first2 = P. | last3 = Kayserili | first3 = H. | last4 = Meguid | first4 = N. A. | last5 = Scott | first5 = E. M. | last6 = Schroth | first6 = J. | last7 = Silhavy | first7 = J. L. | last8 = Kara | first8 = M. | last9 = Khalil | first9 = R. O. | last10 = Ben-Omran | first10 = T. | last11 = Ercan-Sencicek | first11 = A. G. | last12 = Hashish | first12 = A. F. | last13 = Sanders | first13 = S. J. | last14 = Gupta | first14 = A. R. | last15 = Hashem | first15 = H. S. | last16 = Matern | first16 = D. | last17 = Gabriel | first17 = S. | last18 = Sweetman | first18 = L. | last19 = Rahimi | first19 = Y. | last20 = Harris | first20 = R. A. | last21 = State | first21 = M. W. | last22 = Gleeson | first22 = J. G. | title = Mutations in BCKD-kinase Lead to a Potentially Treatable Form of Autism with Epilepsy | doi = 10.1126/science.1224631 | journal = Science | volume = 338 | issue = 6105 | pages = 394–397 | year = 2012 | pmid = 22956686| pmc =3704165 }}

Literature

{{cite journal |vauthors=Paxton R, Harris RA | date = 1982 | title = Isolation of rabbit liver branched chain alpha-ketoacid dehydrogenase and regulation by phosphorylation | journal = J. Biol. Chem. | volume = 257 | pages = 14433–9 | pmid = 7142221 | issue = 23 }}

{{cite journal |vauthors=Wynn RM, Chuang JL, Cote CD, Chuang DT | date = 2000 | title = Tetrameric assembly and conservation in the ATP-binding domain of rat branched-chain alpha-ketoacid dehydrogenase kinase | journal = J. Biol. Chem. | volume = 275 | pages = 30512–9 | pmid = 10903321 | doi = 10.1074/jbc.M005075200 | issue = 39 }}

{{cite journal |vauthors=Chuang JL, Wynn RM, Chuang DT | date = 2002 | title = 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 | journal = J. Biol. Chem. | volume = 277 | pages = 36905–8 | pmid = 12189132 | doi = 10.1074/jbc.C200430200 | issue = 40 }}

{{cite journal |vauthors=Popov KM, Hawes JW, Harris RA | date = 1997 | title = Mitochondrial alpha-ketoacid dehydrogenase kinases: a new family of protein kinases | journal = Adv. Second. Messenger. Phosphoprotein. Res. | volume = 31 | pages = 105–11 | pmid = 9344245 | doi = 10.1016/S1040-7952(97)80012-2 | series = Advances in Second Messenger and Phosphoprotein Research | isbn = 9780120361311 }}

2 : EC 2.7.11|Enzymes of unknown structure