EC 3.4.23.1 - Pepsin A
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 3.4.23.1
Names
Accepted name:
pepsin A
Other
names:
P I
P II
elixir lactate of pepsin
fundus-pepsin
lactated pepsin
lactated pepsin elixir
pepsin
pepsin D
pepsin R
pepsin fortior
P II
elixir lactate of pepsin
fundus-pepsin
lactated pepsin
lactated pepsin elixir
pepsin
pepsin D
pepsin R
pepsin fortior
Systematic name:
Reaction
- Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves Phe1Val, Gln4His, Glu13Ala, Ala14Leu, Leu15Tyr, Tyr16Leu, Gly23Phe, Phe24Phe and Phe25Tyr bonds in the B chain of insulin.
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. Formerly EC 3.4.4.1.
Links to other databases
Enzymes and pathways:
NC-IUBMB
,
BRENDA
,
ExplorEnz
,
ENZYME@ExPASy
,
KEGG
,
MetaCyc
,
MEROPS
,
NIST 74
,
UniPathway
Protein domains and families:
PROSITE:PDOC00128
Gene Ontology:
GO:0004190
CAS Registry Number:
9001-75-6
References
-
Pepsinogen D. A fourth proteolytic zymogen from pig gastric mucosa.Biochem. J. 104 : 735-741 (1967). [PMID: 4167464]
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Pepsin D. A minor component of commercial pepsin preparations.Biochem. J. 104 : 742-748 (1967). [PMID: 4860638]
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Gastric proteinases -structure, function, evolution and mechanism of action.Essays Biochem. 17 : 52-84 (1981). [PMID: 6795036]
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Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 Å resolution.Nature 319 : 33-38 (1986). [PMID: 3941737]
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Aspartyl proteinases.In: Neuberger, A. and Brocklehurst, K. (Eds.)
New Comprehensive Biochemistry , Elsevier , Amsterdam , 1987 , 1-38 -
Evolution in the structure and function of aspartic proteases.J. Cell. Biochem. 33 : 53-63 (1987). [PMID: 3546346]
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Secondary enzyme-substrate interactions: kinetic evidence for ionic interactions between substrate side chains and the pepsin active site.Biochemistry 27 : 4827-4834 (1988). [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]