bonds. High activity on hemoglobin
Reaction: More restricted specificity than pepsin A, but shows preferential cleavage at Tyr bonds. High activity on hemoglobin
Other names: pepsin C; pig parapepsin II; parapepsin II
Comments: Formed from progastricsin, apparently in the gastric juice of most vertebrates. In addition to the fundus, progastricsin is also secreted in antrum and proximal duodenum. Seminal plasma contains a zymogen that is immunologically identical with progastricsin [6]. In peptidase family A1 (pepsin A family). Formerly EC 3.4.4.22
Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, PDB, CAS registry number: 9012-71-9
References:
1. Ryle, A.P. The porcine pepsins and pepsinogens. Methods Enzymol. 19 (1970) 316-336
2. Tang, J. Gastricsin and pepsin. Methods Enzymol. 19 (1970) 406-421
3. Foltmann, B. Gastric proteinases - structure, function, evolution and mechanism of action. Essays Biochem. 17 (1981) 52-84. [PMID: 6795036]
4. Foltmann, B. and Jensen, A.L. Human progastricsin - analysis of intermediates during activation into gastricsin and determination of the amino-acid sequence of the propart. Eur. J. Biochem. 128 (1982) 63-70. [PMID: 6816595]
5. Martin, P., Trieu-Cuot, P., Collin, J.-C. and Ribadeau Dumas, B. Purification and characterization of bovine gastricsin. Eur. J. Biochem. 122 (1982) 31-39. [PMID: 6800788]
6. Reid, W.A., Vongsorasak, L., Svasti, J., Valler, M.J. and Kay J. Identification of the acid proteinase in human seminal fluid as a gastricsin originating in the prostate. Cell Tissue Res. 236 (1984) 597-600. [PMID: 6432332]
7. Hayano, T., Sogawa, K., Ichihara, Y., Fujii-Kuriyama, Y. and Takahasi, K. Primary structure of human pepsinogen C gene. J. Biol. Chem. 263 (1988) 1382-1385. [PMID: 3335549]