Metionilna aminopeptidaza
| Metionilna aminopeptidaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.4.11.18 | ||||||||
| CAS broj | 61229-81-0 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Metionilna aminopeptidaza (EC 3.4.11.18, metioninska aminopeptidaza, peptidaza M, L-metioninska aminopeptidaza, MAP) je enzim.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- Oslobađanje N-terminalne aminokiseline, preferentno metionina, sa peptida i arilamida
Ovaj za membranu vezani enzim je prisutan kod prokariota i eukariota.
Reference
- ↑ Yoshida, A. and Lin, M. (1972). „NH2-terminal formylmethionine- and NH2-terminal methionine-cleaving enzymes in rabbits”. J. Biol. Chem. 247: 952-957. PMID 4110013.
- ↑ Tsunasawa, S., Stewart, J.W. and Sherman, F. (1985). „Acylamino acid-releasing enzyme from rat liver”. J. Biol. Chem. 260: 5832-5391. PMID 2985590.
- ↑ Freitas, J.O., Jr., Termignoni, C. and Guimaraes, J.A. (1985). „Methionine aminopeptidase associated with liver mitochondria and microsomes”. Int. J. Biochem. 17: 1285-1291. PMID 3937747.
- ↑ Ben-Bassat, A., Bauer, K., Chang, S.-Y., Myambo, K., Boosman, A. and Chang, S. (1987). „Processing of the initiation methionine from proteins: properties of Escherichia coli methionine aminopeptidase and its gene structure”. J. Bacteriol. 169: 751-757. PMID 3027045.
- ↑ Roderick, S.L. and Mathews, B.W. (1988). „Crystallization of methionine aminopeptidase from Escherichia coli”. J. Biol. Chem. 263: 16531-16531. PMID 3141408.
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.
Spoljašnje veze
- MeSH Methionyl+aminopeptidase
- 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
