| EC |
3.4.23.19 |
| Accepted name: |
aspergillopepsin II |
| Reaction: |
Preferential cleavage in B chain of insulin: Asn3┼Gln, Gly13┼Ala, Tyr26┼Thr |
| Other name(s): |
proteinase A; proctase A; Aspergillus niger var. macrosporus aspartic proteinase |
| Comments: |
Isolated from Aspergillus niger var. macrosporus, distinct from proteinase B (see aspergillopepsin I) in specificity and insensitivity to pepstatin. In peptidase family G1 (scytalidopepsin B family). Formerly included in EC 3.4.23.6 |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9025-49-4 |
| References: |
| 1. |
Chang, W.-J., Horiuchi, S., Takahashi, K., Yamasaki, M. and Yamada, Y. The structure and function of acid proteases. VI. Effects of acid protease-specific inhibitors on the acid proteases from Aspergillus niger var. macrosporus. J. Biochem. (Tokyo) 80 (1976) 975–981. [PMID: 12156] |
| 2. |
Iio, K. and Yamasaki, M. Specificity of acid proteinase A from Aspergillus niger var. macrosporus towards B-chain of performic acid oxidized bovine insulin. Biochim. Biophys. Acta 429 (1976) 912–924. [DOI] [PMID: 1268233] |
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| [EC 3.4.23.19 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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