Arginaza
| Arginaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Arginaza 1, trimer, Rattus norvegicus | |||||||||
| Identifikatori | |||||||||
| EC broj | 3.5.3.1 | ||||||||
| CAS broj | 9000-96-8 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Arginaza (EC 3.5.3.1, argininska amidinaza, kanavanaza, L-arginaza, argininska transamidinaza) je enzim sa sistematskim imenom L-arginin amidinohidrolaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- L-arginin + H2O L-ornitin + ureja
Ovaj enzim takođe hidrolizuje alfa-N-supstituisane L-arginine i kanavanin.
Reference
- ↑ Bach, S.J. and Killip, J.D. (1961). „Studies on the purification and the kinetic properties of arginase from beef, sheep and horse liver”. Biochim. Biophys. Acta 47: 336-343. PMID 13685626.
- ↑ Cabello, J., Basilio, C. and Prajoux, V. (1961). „Kinetic properties of erythrocyte- and liver arginase”. Biochim. Biophys. Acta 48: 148-152. PMID 13689647.
- ↑ Dumitru, I.F. (1973). „Study of L-arginine amidinohydrolase from vegetable origin. Purification, crystallization and molecular weight”. Acta Vitamin. Enzymol. 27: 207-210. PMID 4801830.
- ↑ Greenberg, D.M. (1960). „Arginase”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 4 (2nd izd.). New York: Academic Press. str. 257-267.
- ↑ Greenberg, D.M., Bagot, A.E. and Roholt, O.A. (1956). „Liver arginase. III. Properties of highly purified arginase”. Arch. Biochem. Biophys. 62: 446-453. PMID 13328133.
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.
- Greenberg, D.M. (1960). „Arginase”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 4 (2nd izd.). New York: Academic Press. str. 257-267.
Vanjske veze
- MeSH Arginase
- 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
