Dihidrolipoilizinski-ostatak (2-metilpropanoil)transferaza
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| Dihidrolipoilizinski-ostatak (2-metilpropanoil)transferaza | |||||||||
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| Identifikatori | |||||||||
| EC broj | 2.3.1.168 | ||||||||
| CAS broj | 102784-26-9 | ||||||||
| 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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Dihidrolipoilizinski-ostatak (2-metilpropanoil)transferaza (EC 2.3.1.168, dihidrolipoil transacilaza, enzim-dihidrolipoillizin:2-metilpropanoil-KoA S-(2-metilpropanoil)transferaza, 2-metilpropanoil-KoA:enzim-6-N-(dihidrolipoil)lizin S-(2-metilpropanoil)transferaza) je enzim sa sistematskim imenom 2-metilpropanoil-KoA:enzim-N6-(dihidrolipoil)lizin S-(2-metilpropanoil)transferaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- 2-metilpropanoil-KoA + enzim N6-(dihidrolipoil)lizin KoA + enzim N6-(S-[2-metilpropanoil]dihidrolipoil)lizin
Ova enzim je multimer (24-mer). On formira osnovu multienzimskog kompleksa 3-metil-2-oksobutanoat dehidrogenaze, i čvrsto vezuje EC 1.2.4.4, 3-metil-2-oksobutanoat dehidrogenazu (2-metilpropanoil-transfer) i EC 1.8.1.4, dihidrolipoil dehidrogenazu.
Reference[uredi | uredi kod]
- ↑ Massey, L.K., Sokatch, J.R. and Conrad, R.S. (1976). „Branched-chain amino acid catabolism in bacteria”. Bacteriol. Rev. 40: 42-54. PMID 773366.
- ↑ Chuang, D.T., Hu, C.C., Ku, L.S., Niu, W.L., Myers, D.E. and Cox, R.P. (1984). „Catalytic and structural properties of the dihydrolipoyl transacylase component of bovine branched-chain α-keto acid dehydrogenase”. J. Biol. Chem. 259: 9277-9284. PMID 6746648.
- ↑ Wynn, R.M., Davie, J.R., Zhi, W., Cox, R.P. and Chuang, D.T. (1994). „In vitro reconstitution of the 24-meric E2 inner core of bovine mitochondrial branched-chain α-keto acid dehydrogenase complex: requirement for chaperonins GroEL and GroES”. Biochemistry 33: 8962-8968. PMID 7913832.
- ↑ Perham, R.N. (2000). „Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions”. Annu. Rev. Biochem. 69: 961-1004. PMID 10966480.
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.