KEGG   ENZYME: 3.4.23.1Help
Entry
EC 3.4.23.1                 Enzyme                                 

Name
pepsin A;
pepsin;
lactated pepsin;
pepsin fortior;
fundus-pepsin;
elixir lactate of pepsin;
P I;
lactated pepsin elixir;
P II;
pepsin R;
pepsin D
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Aspartic endopeptidases
BRITE hierarchy
Reaction(IUBMB)
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
Comment
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.
History
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
Orthology
K06002  
pepsin A
Genes
HSA: 
5222(PGA5) 643834(PGA3) 643847(PGA4)
PTR: 
738012(PGA4)
PPS: 
100973723(PGA5)
GGO: 
PON: 
MCC: 
694562(PGA4) 694706(PGA4)
MCF: 
MMU: 
58803(Pga5)
RNO: 
CGE: 
TUP: 
CFA: 
AML: 
FCA: 
PTG: 
BTA: 
337904(PAG10) 337906(PAG12) 414350(PGA5) 784113
BOM: 
PHD: 
CHX: 
SSC: 
CFR: 
BACU: 
LVE: 
ECB: 
MYB: 
MYD: 
PALE: 
GGA: 
395691(PGA)
MGP: 
TGU: 
FAB: 
PHI: 
FPG: 
FCH: 
CLV: 
ASN: 
AMJ: 
PSS: 
CMY: 
ACS: 
XLA: 
373564(pga4)
XTR: 
496914(pga4)
TRU: 
777954(pga)
MZE: 
LCM: 
CME: 
GSL: 
MAJ: 
CCI: 
PFA: 
PFH: 
PYO: 
PCB: 
PBE: 
PKN: 
PVX: 
PCY: 
TAN: 
TPV: 
BBO: 
BBOV_IV007890(23.m06476)
BEQ: 
TGO: 
 » show all
Taxonomy
Reference
1  [PMID:4167464]
  Authors
Lee D, Ryle AP.
  Title
Pepsinogen D. A fourth proteolytic zymogen from pig gastric mucosa.
  Journal
Biochem. J. 104 (1967) 735-41.
  Organism
Sus scofa
Reference
2  [PMID:4860638]
  Authors
Lee D, Ryle AP.
  Title
Pepsin D. A minor component of commercial pepsin preparations.
  Journal
Biochem. J. 104 (1967) 742-8.
  Organism
Sus scofa
Reference
3  [PMID:6795036]
  Authors
Foltmann B.
  Title
Gastric proteinases--structure, function, evolution and mechanism of action.
  Journal
Essays. Biochem. 17 (1981) 52-84.
Reference
4  [PMID:3941737]
  Authors
James MN, Sielecki AR.
  Title
Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 A resolution.
  Journal
Nature. 319 (1986) 33-8.
  Organism
Sus scofa
Reference
5
  Authors
Fruton, J.S.
  Title
Aspartyl proteinases.
  Journal
In: Neuberger, A. and Brocklehurst, K. (Eds.), New Comprehensive Biochemistry: Hydrolytic Enzymes, vol. 16, Elsevier, Amsterdam, 1987, p. 1-38.
Reference
6  [PMID:3546346]
  Authors
Tang J, Wong RN.
  Title
Evolution in the structure and function of aspartic proteases.
  Journal
J. Cell. Biochem. 33 (1987) 53-63.
  Organism
Homo sapiens, Bos taurus, Sus scofa
Reference
7  [PMID:3139029]
  Authors
Pohl J, Dunn BM.
  Title
Secondary enzyme-substrate interactions: kinetic evidence for ionic interactions between substrate side chains and the pepsin active site.
  Journal
Biochemistry. 27 (1988) 4827-34.
  Organism
Sus scofa
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9001-75-6

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