KEGG   ENZYME: 3.4.23.22Help
Entry
EC 3.4.23.22                Enzyme                                 

Name
endothiapepsin;
Endothia aspartic proteinase;
Endothia acid proteinase;
Endothia parasitica acid proteinase;
Endothia parasitica aspartic proteinase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Aspartic endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Hydrolysis of proteins with specificity similar to that of pepsin A; prefers hydrophobic residues at P1 and P1', but does not cleave Ala14-Leu in the B chain of insulin or Z-Glu-Tyr. Clots milk
Comment
From the ascomycete Endothia parasitica. In peptidase family A1 (pepsin A family).
History
EC 3.4.23.22 created 1992 (EC 3.4.23.6 created 1992 (EC 3.4.23.6 created 1961 as EC 3.4.4.17, transferred 1972 to EC 3.4.23.6, modified 1981 [EC 3.4.23.7, EC 3.4.23.8, EC 3.4.23.9, EC 3.4.23.10, EC 3.4.99.1, EC 3.4.99.15 and EC 3.4.99.25 all created 1972 and incorporated 1978], part incorporated 1992)
Orthology
K20737  
endothiapepsin
Reference
1
  Authors
Whitaker, J.R.
  Title
Protease of Endothia parasitica.
  Journal
Methods Enzymol. 19 (1970) 436-445.
Reference
2  [PMID:4552802]
  Authors
Williams DC, Witaker JR, Caldwell PV.
  Title
Hydrolysis of peptide bonds of the oxidized B-chain of insulin by Endothia parasitica protease.
  Journal
Arch. Biochem. Biophys. 149 (1972) 52-61.
Reference
3  [PMID:3305016]
  Authors
Barkholt V.
  Title
Amino acid sequence of endothiapepsin. Complete primary structure of the aspartic protease from Endothia parasitica.
  Journal
Eur. J. Biochem. 167 (1987) 327-38.
  Sequence
Reference
4  [PMID:3119339]
  Authors
Cooper J, Foundling S, Hemmings A, Blundell T, Jones DM, Hallett A, Szelke M.
  Title
The structure of a synthetic pepsin inhibitor complexed with endothiapepsin.
  Journal
Eur. J. Biochem. 169 (1987) 215-21.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
37205-60-0

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