EC |
3.4.23.28 |
Accepted name: |
acrocylindropepsin |
Reaction: |
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 |
Other name(s): |
Acrocylindrium proteinase; Acrocylindrium acid proteinase |
Comments: |
From the imperfect fungus Acrocylindrium sp. Has a very low pH optimum on casein of 2.0. In peptidase family A1 (pepsin A family). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-84-9 |
References: |
1. |
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. |
2. |
Ichihara, S. and Uchino, F. The specificity of acid proteinase from Acrocylindrium. Agric. Biol. Chem. 39 (1975) 423–428. |
3. |
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] |
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[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)] |
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