|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 220.127.116.11
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.
Mass balance status: The left side is missing: Peptides: 2 . The right side is missing: Proteins: 1 O: 1 H: 1
Enzyme Commission Primary Name: aspergillopepsin II
Enzyme Commission Synonyms: proteinase A, proctase A, Aspergillus niger var. macrosporus aspartic proteinase
Taxonomic Range: Fungi
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): 36.144756 [Latendresse13]
Enzyme Commission Summary:
This enzyme catalyzes preferential cleavage in B chain of insulin : Asn3-|-Gln, Gly13-|-Ala, Tyr26-|-Thr.
Isolated from Aspergilus 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 18.104.22.168.
Chang76: Chang WJ, Horiuchi S, Takahashi K, Yamasaki M, Yamada Y (1976). "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 80(5);975-81. PMID: 12156
Iio76: Iio K, Yamasaki M (1976). "Specificity of acid proteinase A from Aspergillus niger var. macrosporus towards B-chain of performic acid oxidized bovine insulin." Biochim Biophys Acta 429(3);912-24. PMID: 1268233
©2015 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493