Aminopeptidaza S
| Aminopeptidaza S | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.4.11.24 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Aminopeptidaza S (EC 3.4.11.24, Mername-AA022 peptidaza, SGAP, aminopeptidaza (Streptomyces griseus), Streptomyces griseus aminopeptidaza, S. griseus AP, dvostruka-cinkova aminopeptidaza) je enzim sa sistematskim imenom '.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- Oslobađanje N-terminalne aminokiseline sa preferencijom za velike hidrofobne amino-terminuske ostatke
Aminopeptidaze imaju mnoštovo bioloških funkcija, uključujući maturaciju proteina, proteinsku degradaciju, kontrolu ćelijskog ciklusa i regulaciju hormonskih nivoa.
Reference
- ↑ Spungin, A. and Blumberg, S. (1989). „Streptomyces griseus aminopeptidase is a calcium-activated zinc metalloprotein. Purification and properties of the enzyme”. Eur. J. Biochem. 183: 471-477. PMID 2503378.
- ↑ Ben-Meir, D., Spungin, A., Ashkenazi, R. and Blumberg, S. (1993). „Specificity of Streptomyces griseus aminopeptidase and modulation of activity by divalent metal ion binding and substitution”. Eur. J. Biochem. 212: 107-112. PMID 8444149.
- ↑ Arima, J., Uesugi, Y., Iwabuchi, M. and Hatanaka, T. (2006). „Study on peptide hydrolysis by aminopeptidases from Streptomyces griseus, Streptomyces septatus and Aeromonas proteolytica”. Appl. Microbiol. Biotechnol. 70: 541-547. PMID 16080009.
- ↑ Fundoiano-Hershcovitz, Y., Rabinovitch, L., Langut, Y., Reiland, V., Shoham, G. and Shoham, Y. (2004). „Identification of the catalytic residues in the double-zinc aminopeptidase from Streptomyces griseus”. FEBS Lett. 571: 192-196. PMID 15280041.
- ↑ Gilboa, R., Greenblatt, H.M., Perach, M., Spungin-Bialik, A., Lessel, U., Wohlfahrt, G., Schomburg, D., Blumberg, S. and Shoham, G. (2000). „Interactions of Streptomyces griseus aminopeptidase with a methionine product analogue: a structural study at 1.53 Å resolution”. Acta Crystallogr. D Biol. Crystallogr. 56: 551-558. PMID 10771423.
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 Aminopeptidase+S
- 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
