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
Uchino, F., Kurono, Y. and Doi, S. Purification and some properties of crystalline acid protease from Acrocylindrium sp. Agric. Biol. Chem.31 (1967) 428–434.
Ichihara, S. and Uchino, F. The specificity of acid proteinase from Acrocylindrium. Agric. Biol. Chem.39 (1975) 423–428.
Takahashi, K. and Chang, W.-J. 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. J. Biochem. (Tokyo)80 (1976) 497–506. [PMID: 10290]
[EC 18.104.22.168 created 1992 (EC 22.214.171.124 created 1992 (EC 126.96.36.199 created 1961 as EC 188.8.131.52, transferred 1972 to EC 184.108.40.206, modified 1981 [EC 220.127.116.11, EC 18.104.22.168, EC 22.214.171.124, EC 126.96.36.199, EC 188.8.131.52, EC 184.108.40.206 and EC 220.127.116.11 all created 1972 and incorporated 1978], part incorporated 1992)]