(3-Metil-2-oksobutanoat dehidrogenaza (acetil-transfer)) kinaza
(Preusmjereno sa stranice BCODH kinaza)
(3-metil-2-oksobutanoat dehidrogenaza (acetil-transfer)) kinaza | |||||||||
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Identifikatori | |||||||||
EC broj | 2.7.11.4 | ||||||||
CAS broj | 82391-38-6 | ||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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(3-metil-2-oksobutanoat dehidrogenaza (acetil-transfer)) kinaza (EC 2.7.11.4, BCK, BCKD kinaza, BCODH kinaza, dehidrogenazna kinaza alfa-ketokiselina razgranatog lanca, dehidrogenazna kinaza 2-okso kiselina razgranatog lanca, dehidrogenazna kinaza keto kiselina razgranatog lanca, dehidrogenazna kinaza okso kiselina razgranatog lanca (fosforilacija), STK2) je enzim sa sistematskim imenom ATP:(3-metil-2-oksobutanoat dehidrogenaza (acetil-transfer)) fosfotransferaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- ATP + [3-metil-2-oksobutanoat dehidrogenaza (acetil-transfer)] ADP + [3-metil-2-oksobutanoat dehidrogenaza (acetil-transfer)] fosfat
Ovaj enzim nema aktivirajuće jedinjenje ali je specifičan za svoj supstrat.
Reference[uredi | uredi kod]
- ↑ Paxton, R. and Harris, R.A. (1982). „Isolation of rabbit liver branched chain α-ketoacid dehydrogenase and regulation by phosphorylation”. J. Biol. Chem. 257: 14433-14439. PMID 7142221.
- ↑ Wynn, R.M., Chuang, J.L., Cote, C.D. and Chuang, D.T. (2000). „Tetrameric assembly and conservation in the ATP-binding domain of rat branched-chain α-ketoacid dehydrogenase kinase”. J. Biol. Chem. 275: 30512-30519. PMID 10903321.
- ↑ Chuang, J.L., Wynn, R.M. and Chuang, D.T. (2002). „The C-terminal hinge region of lipoic acid-bearing domain of E2b is essential for domain interaction with branched-chain α-keto acid dehydrogenase kinase”. J. Biol. Chem. 277: 36905-36908. PMID 12189132.
- ↑ Popov, K.M., Hawes, J.W. and Harris, R.A. (1997). „Mitochondrial α-ketoacid dehydrogenase kinases: a new family of protein kinases”. Adv. Second Messenger Phosphoprotein Res. 31: 105-111. PMID 9344245.
Literatura[uredi | uredi kod]
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.