Pepsin-A
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
| Pepsin-A | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Pepsin, Human | |||||||||
| Identifikatori | |||||||||
| EC broj | 3.4.23.1 | ||||||||
| CAS broj | 9001-75-6 | ||||||||
| Baze podataka | |||||||||
| IntEnz | IntEnz pregled | ||||||||
| BRENDA | BRENDA pristup | ||||||||
| ExPASy | NiceZyme pregled | ||||||||
| KEGG | KEGG pristup | ||||||||
| MetaCyc | metabolički put | ||||||||
| PRIAM | profil | ||||||||
| Strukture PBP | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- 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 уреди
- ^ Lee, D. & Ryle, A.P. (1967). „Pepsinogen D. A fourth proteolytic zymogen from pig gastric mucosa”. Biochem. J. 104: 735—741. PMID 4167464.
- ^ Lee, D. & 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. & 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”. Ур.: Neuberger, A. and Brocklehurst, K. New Comprehensive Biochemistry: Hydrolytic Enzymes. 16. Amsterdam: Elsevier. стр. 1—38.
- ^ Tang, J. & Wong, R.N.S. (1987). „Evolution in the structure and function of aspartic proteases”. J. Cell. Biochem. 33: 53—63. PMID 3546346.
- ^ Pohl, J. & 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.
Литература уреди
- Fruton, J.S. (1987). „Aspartyl proteinases”. Ур.: Neuberger, A. and Brocklehurst, K. New Comprehensive Biochemistry: Hydrolytic Enzymes. 16. Amsterdam: Elsevier. стр. 1—38.
