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: 107966244
PPS: 100973723(PGA5)
GGO: 101127189 101127800 109028881
PON: 100294580(PG) 100443904
NLE: 100584713(PGA4) 100585031 100587784(PGA5)
MCC: 694562(PGA4) 694706
MCF: 102141063 102141865(PGA4)
CSAB: 103234519 103234533 103241962
RRO: 104677990 104679397
CJC: 100385980(PGA) 100414683
SBQ: 101046858
MMU: 58803(Pga5)
RNO: 108348129 60372(Pga5)
CGE: 100765022
NGI: 103725401
CCAN: 109686117
CFA: 403711(PGA) 483802
ORO: 101370837
BTA: 281964(PAG1) 337896(PAG3) 337897(PAG2) 337898(PAG4) 337899(PAG5) 337900(PAG6) 337901(PAG7) 337902(PAG8) 337903(PAG9) 337904(PAG10) 337906(PAG12) 337907(PAG11) 337908(PAG14) 337909(PAG15) 337910(PAG16) 337911(PAG18) 337912(PAG17) 337913(PAG19) 337914(PAG20) 337915(PAG21) 414350(PGA5) 504812 517463(MGC157408) 518205(MGC157405) 520130 521902 524173 528815 536947 613739 614287 784867
SSC: 100523770 100737419 396749(PAG6) 396892(PGA5)
CDK: 105094886(pepsin) 105094888
MYB: 102253898
RSS: 109459502
GGA: 100857834 395691(PGA5)
TGU: 100231572
GFR: 102037280
FAB: 101814802
PHI: 102102519
PMAJ: 107206062
CCW: 104684125(PGA3)
FPG: 101924478
FCH: 102059794
CLV: 102088393 102093714(PGA5)
EGZ: 104122976
CMY: 102937464
ACS: 100567277
PVT: 110078337
GJA: 107120366
XLA: 108704873 373564(pga4.L)
XTR: 101732307 496914(pga4)
NPR: 108797363
AMEX: 103025805
TRU: 777954(pga)
LCO: 104926693 104929130(pepsin)
MZE: 101463839
PYO: PY17X_1225700(PY06692)
PCB: PCHAS_122310(PC000654.04.0)
BBO: BBOV_IV007890(23.m06476)
TGO: TGME49_246550(ASP3)
SMIN: v1.2.006346.t1(symbB.v1.2.006346.t1) v1.2.007067.t1(symbB.v1.2.007067.t1)
 » 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 104:735-41 (1967)
Reference
2  [PMID:4860638]
  Authors
Lee D, Ryle AP.
  Title
Pepsin D. A minor component of commercial pepsin preparations.
  Journal
Biochem J 104:742-8 (1967)
Reference
3  [PMID:6795036]
  Authors
Foltmann B.
  Title
Gastric proteinases--structure, function, evolution and mechanism of action.
  Journal
Essays Biochem 17:52-84 (1981)
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 319:33-8 (1986)
DOI:10.1038/319033a0
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 33:53-63 (1987)
DOI:10.1002/jcb.240330106
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 27:4827-34 (1988)
Other DBs
ExplorEnz - The Enzyme Database: 3.4.23.1
IUBMB Enzyme Nomenclature: 3.4.23.1
ExPASy - ENZYME nomenclature database: 3.4.23.1
BRENDA, the Enzyme Database: 3.4.23.1
CAS: 9001-75-6

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