Karboksipeptidaza E
| Karboksipeptidaza E | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.4.17.10 | ||||||||
| CAS broj | 81876-95-1 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Karboksipeptidaza E (EC 3.4.17.10, karboksipeptidaza H, enkefalinska konvertaza, kobaltom stimulisana hromafin granularna karboksipeptidaza, enkefalinska konvertaza, membranska karboksipeptidaza, enkefalinska prekursorska endopeptidaza, enkefalinska prekursorska karboksipeptidaza, peptidilna-L-lizin(-L-arginin) hidrolaza) je enzim.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- Odvajanje C-terminalnog arginina ili lizina sa polipeptida
Ovaj cinkov enzim aktivira jon Co2+.
Reference
- ↑ Qian, Y.M., Varlamov, O. and Fricker, L.D. (1999). „Glu300 of rat carboxypeptidase E is essential for enzymatic activity but not substrate binding or routing to the regulated secretory pathway”. J. Biol. Chem. 274: 11582-11586. PMID 10206965.
- ↑ Fricker, L.D. (1998). „Carboxypeptidase E/H”. u: Barrett, A.J., Rawlings, N.D. and Woessner, J.F.. Handbook of Proteolytic Enzymes. London: Academic Press. str. 1341-1344.
- ↑ Fricker, L.D. (1995). „Methods for studying carboxypeptidase E”. Methods Neurosci. 23: 237-250.
- ↑ Manser, E., Fernandez, D. (1990). „, Loo,L., Goh, P.Y., Monfries, C., Hall, C. and Lim, L. Human carboxypeptidase E: isolation and characterisaton of the cDNA, sequence conservation, expression and processing in vitro”. Biochem. J. 267: 517-525. PMID 2334405.
- ↑ Fricker, L.D. (1988). „Carboxypeptidase E”. Annu. Rev. Physiol. 50: 309-321. PMID 2897826.
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.
- Fricker, L.D. (1998). „Carboxypeptidase E/H”. u: Barrett, A.J., Rawlings, N.D. and Woessner, J.F.. Handbook of Proteolytic Enzymes. London: Academic Press. str. 1341-1344.
Spoljašnje veze
- MeSH Carboxypeptidase+E
- 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
