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Open Access Articles- Top Results for (3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring))

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

[3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] kinase
Identifiers
EC number 2.7.11.4
CAS number 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 / EGO

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)] <math>\rightleftharpoons</math> 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

  1. ^ doi:10.1126/science.1224631
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  • 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. PMID 10903321. doi:10.1074/jbc.M005075200. 
  • 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. PMID 12189132. doi:10.1074/jbc.C200430200. 
  • 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. ISBN 9780120361311. PMID 9344245. doi:10.1016/S1040-7952(97)80012-2. 


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