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
- 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
- Fruton, J.S. (1987). „Aspartyl proteinases”. u: Neuberger, A. and Brocklehurst, K.. New Comprehensive Biochemistry: Hydrolytic Enzymes. 16. Amsterdam: Elsevier. str. 1-38.
Vanjske veze
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