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Entry
EC 3.4.23.19                Enzyme                                 

Name
aspergillopepsin II;
proteinase A;
proctase A;
Aspergillus niger var. macrosporus aspartic proteinase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Aspartic endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Preferential cleavage in B chain of insulin: Asn3!Gln, Gly13!Ala, Tyr26!Thr
Comment
Isolated from Aspergillus niger var. macrosporus, distinct from proteinase B (see aspergillopepsin I) in specificity and insensitivity to pepstatin. In peptidase family A4 (scytalidopepsin B family). Formerly included in EC 3.4.23.6
History
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)
Reference
1  [PMID:12156]
  Authors
Chang WJ, Horiuchi S, Takahashi K, Yamasaki M, Yamada Y.
  Title
The structure and function of acid proteases. VI. Effects of acid protease-specific inhibitors on the acid proteases from Aspergillus niger var. macrosporus.
  Journal
J Biochem (Tokyo) 80:975-81 (1976)
Reference
2  [PMID:1268233]
  Authors
Iio K, Yamasaki M.
  Title
Specificity of acid proteinase A from Aspergillus niger var. macrosporus towards B-chain of performic acid oxidized bovine insulin.
  Journal
Biochim Biophys Acta 429:912-24 (1976)
DOI:10.1016/0005-2744(76)90336-3
Other DBs
ExplorEnz - The Enzyme Database: 3.4.23.19
IUBMB Enzyme Nomenclature: 3.4.23.19
ExPASy - ENZYME nomenclature database: 3.4.23.19
BRENDA, the Enzyme Database: 3.4.23.19
CAS: 9025-49-4

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