Acetil-KoA karboksilaza
| Acetil-KoA karboksilaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifikatori | |||||||||
| EC broj | 6.4.1.2 | ||||||||
| CAS broj | 9023-93-2 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Acetil-KoA karboksilaza (EC 6.4.1.2, acetil koenzim A karboksilaza) je enzim sa sistematskim imenom acetil-KoA:ugljen-dioksid ligaza (formira ADP).[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- ATP + acetil-KoA + HCO3- ADP + fosfat + malonil-KoA
Ovaj biotinilni protein takođe katalizuje transkarboksilaciju.
Reference
- ↑ Hatch, M.D. and Stumpf, P.K. (1961). „Fat metabolism in higher plants. XVI. Acetyl coenzyme A carboxylase and acyl coenzyme A-malonyl coenzyme A transcarboxylase from wheat germ”. J. Biol. Chem. 236: 2879-2885. PMID 13905314.
- ↑ Matsuhashi, M., Matsuhashi, S. and Lynen, F. (1964). „Zur Biosynthese der Fettsäuren. V. Die Acetyl-CoA Carboxylase aus Rattenleber und ihre Aktivierung durch Citronsäure”. Biochem. Z. 340: 263-289. PMID 14317958.
- ↑ Matsuhashi, M., Matsuhashi, S., Numa, S. and Lynen, F. (1964). „[On the biosynthesis of fatty acids. IV. Acetyl-CoA carboxylase from yeast.]”. Biochem. Z. 340: 243-262. PMID 14317957.
- ↑ Vagelos, P. (1971). „Regulation of fatty acid biosynthesis”. Curr. Top. Cell. Regul. 4: 119-166.
- ↑ Wakil, S.J. (1958). „A malonic acid derivative as an intermediate in fatty acid synthesis”. J. Am. Chem. Soc. 80: 6465-6465.
Literatura
- 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.
Vanjske veze
- MeSH Acetyl-CoA+carboxylase
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
