ExplorEnz: EC 3.4.23.1

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3.4.23.1

Accepted name:

pepsin A

Reaction:

Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1′ positions. Cleaves Phe¹┼Val, Gln⁴┼His, Glu¹³┼Ala, Ala¹⁴┼Leu, Leu¹⁵┼Tyr, Tyr¹⁶┼Leu, Gly²³┼Phe, Phe²⁴┼Phe and Phe²⁵┼Tyr bonds in the B chain of insulin

Other name(s):

pepsin; lactated pepsin; pepsin fortior; fundus-pepsin; elixir lactate of pepsin; P I; lactated pepsin elixir; P II; pepsin R; pepsin D

Comments:

The predominant endopeptidase in the gastric juice of vertebrates, formed from pepsinogen A by limited proteolysis. Human pepsin A occurs in five molecular forms. Pig pepsin D [1,2] is unphosphorylated pepsin A. Type example of peptidase family A1.

Links to other databases:

BRENDA, EXPASY, GTD, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9001-75-6

References:

1.	Lee, D. and Ryle, A.P. Pepsinogen D. A fourth proteolytic zymogen from pig gastric mucosa. Biochem. J. 104 (1967) 735–741. [PMID: 4167464]
2.	Lee, D. and Ryle, A.P. Pepsin D. A minor component of commercial pepsin preparations. Biochem. J. 104 (1967) 742–748. [PMID: 4860638]
3.	Foltmann, R. Gastric proteinases -structure, function, evolution and mechanism of action. Essays Biochem. 17 (1981) 52–84. [PMID: 6795036]
4.	James, M.N.G. and Sielecki, A.R. Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 Å resolution. Nature 319 (1986) 33–38. [DOI] [PMID: 3941737]
5.	Fruton, J.S. Aspartyl proteinases. In: Neuberger, A. and Brocklehurst, K. (Ed.), New Comprehensive Biochemistry: Hydrolytic Enzymes, vol. 16, Elsevier, Amsterdam, 1987, pp. 1–38.
6.	Tang, J. and Wong, R.N.S. Evolution in the structure and function of aspartic proteases. J. Cell. Biochem. 33 (1987) 53–63. [DOI] [PMID: 3546346]
7.	Pohl, J. and Dunn, B.M. Secondary enzyme-substrate interactions: kinetic evidence for ionic interactions between substrate side chains and the pepsin active site. Biochemistry 27 (1988) 4827–4834. [PMID: 3139029]

[EC 3.4.23.1 created 1961 as EC 3.4.4.1, transferred 1972 to EC 3.4.23.1, modified 1986, modified 1989]