Hydrolases;
Acting on peptide bonds (peptidases);
Aspartic endopeptidases
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 31:428-434 (1967)
Reference
2
Authors
Ichihara, S. and Uchino, F.
Title
The specificity of acid proteinase from Acrocylindrium.
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.
