ExplorEnz: EC 3.4.23.3

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3.4.23.3

Accepted name:

gastricsin

Reaction:

More restricted specificity than pepsin A, but shows preferential cleavage at Tyr┼ bonds. High activity on hemoglobin

Other name(s):

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).

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, MEROPS, 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. [DOI] [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. [DOI] [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]

[EC 3.4.23.3 created 1965 as EC 3.4.4.22, transferred 1972 to EC 3.4.23.3, modified 1986]