KEGG   ENZYME: 3.4.23.28Help
Entry
EC 3.4.23.28                Enzyme                                 

Name
acrocylindropepsin;
Acrocylindrium proteinase;
Acrocylindrium acid proteinase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Aspartic endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Preference for hydrophobic residues at P1 and P1'. Action on the B chain of insulin is generally similar to that of pepsin A, but it also cleaves Leu6!Cys(SO3H), Glu21!Arg and Asn3!Gln, although not Gln4-His
Comment
From the imperfect fungus Acrocylindrium sp. Has a very low pH optimum on casein of 2.0. In peptidase family A1 (pepsin A family).
History
EC 3.4.23.28 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)
Reference
1
  Authors
Uchino, F., Kurono, Y. and Doi, S.
  Title
Purification and some properties of crystalline acid protease from Acrocylindrium sp.
  Journal
Agric. Biol. Chem. 31 (1967) 428-434.
Reference
2
  Authors
Ichihara, S. and Uchino, F.
  Title
The specificity of acid proteinase from Acrocylindrium.
  Journal
Agric. Biol. Chem. 39 (1975) 423-428.
Reference
3  [PMID:10290]
  Authors
Takahashi K, Chang WJ.
  Title
The structure and function of acid proteases. V. Comparative studies on the specific inhibition of acid proteases by diazoacetyl-DL-norleucine methyl ester, 1,2-epoxy-3-(p-nitrophenoxy) propane and pepstatin.
  Journal
J. Biochem. (Tokyo). 80 (1976) 497-506.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
37288-84-9

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