Pepsin-A
| Pepsin-A | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Pepsin, Human | |||||||||
| Identifikatori | |||||||||
| EC broj | 3.4.23.1 | ||||||||
| CAS broj | 9001-75-6 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Pepsin-A (EC 3.4.23.1, pepsin, laktatedni pepsin, pepsinski fortior, fundus-pepsin, eliksir laktatnog pepsina, P I, laktatedno pepsinski eliksir, P II, pepsin R, pepsin D) je enzim.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
- Preferentno razlaganje: hidrofobnih, preferentno aromatičnih, ostataka u P1 i P1' pozicijama. Razlaganje Phe1-Val, Gln4-His, Glu13-Ala, Ala14-Leu, Leu15-Tyr, Tyr16-Leu, Gly23-Phe, Phe24-Phe i Phe25-Tyr veza u B lancima insulina
Ovaj enzim je predominantna endopeptidaza u gastričnom soku kičmenjaka.
Reference
- ↑ Lee, D. and Ryle, A.P. (1967). „Pepsinogen D. A fourth proteolytic zymogen from pig gastric mucosa”. Biochem. J. 104: 735-741. PMID 4167464.
- ↑ Lee, D. and Ryle, A.P. (1967). „Pepsin D. A minor component of commercial pepsin preparations”. Biochem. J. 104: 742-748. PMID 4860638.
- ↑ Foltmann, R. (1981). „Gastric proteinases -structure, function, evolution and mechanism of action”. Essays Biochem. 17: 52-84. PMID 6795036.
- ↑ James, M.N.G. and Sielecki, A.R. (1986). „Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 Å resolution”. Nature 319: 33-38. PMID 3941737.
- ↑ Fruton, J.S. (1987). „Aspartyl proteinases”. u: Neuberger, A. and Brocklehurst, K.. New Comprehensive Biochemistry: Hydrolytic Enzymes. 16. Amsterdam: Elsevier. str. 1-38.
- ↑ Tang, J. and Wong, R.N.S. (1987). „Evolution in the structure and function of aspartic proteases”. J. Cell. Biochem. 33: 53-63. PMID 3546346.
- ↑ Pohl, J. and Dunn, B.M. (1988). „Secondary enzyme-substrate interactions: kinetic evidence for ionic interactions between substrate side chains and the pepsin active site”. Biochemistry 27: 4827-4834. PMID 3139029.
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.
- Fruton, J.S. (1987). „Aspartyl proteinases”. u: Neuberger, A. and Brocklehurst, K.. New Comprehensive Biochemistry: Hydrolytic Enzymes. 16. Amsterdam: Elsevier. str. 1-38.
Spoljašnje veze
- MeSH Pepsin+A
- 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
