The Enzyme Database

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Accepted name: oryzin
Reaction: Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt > Ac-Tyr-OEt. Does not hydrolyse peptide amides
Other name(s): Aspergillus alkaline proteinase; aspergillopeptidase B; API 21; aspergillopepsin B; aspergillopepsin F; Aspergillus candidus alkaline proteinase; Aspergillus flavus alkaline proteinase; Aspergillus melleus semi-alkaline proteinase; Aspergillus oryzae alkaline proteinase; Aspergillus parasiticus alkaline proteinase; Aspergillus serine proteinase; Aspergillus sydowi alkaline proteinase; Aspergillus soya alkaline proteinase; Aspergillus melleus alkaline proteinase; Aspergillus sulphureus alkaline proteinase; prozyme; P 5380; kyorinase; seaprose S; semi-alkaline protease; sumizyme MP; prozyme 10; onoprose; onoprose SA; protease P; promelase
Comments: A peptidase of family S8 (subtilisin family), not containing cysteine, that is the predominant extracellular alkaline endopeptidase of the mold Aspergillus oryzae. Identical or closely related enzymes are produced by A. flavus and A. sojae [2,3,4]
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9074-07-1
1.  Nakagawa, Y. Alkaline proteinases from Aspergillus. Methods Enzymol. 19 (1970) 581–591.
2.  Hayashi, K. and Terada, M. Some characteristics of hydrolysis of synthetic substrates and proteins by the alkaline proteases from Aspergillus sojae. Agric. Biol. Chem. 36 (1972) 1755–1765.
3.  Turková, J., Mikes, O., Hayashi, K., Danno, G. and Polgár, L. Alkaline proteinases of the genus Aspergillus. Biochim. Biophys. Acta 257 (1972) 257–263. [DOI] [PMID: 4623338]
4.  Morihara, K., Oka, T. and Tsuzuki, H. Comparative study of various serine alkaline proteinases from microorganisms. Esterase activity against N-acylated peptide ester substrates. Arch. Biochem. Biophys. 165 (1974) 72–79. [DOI] [PMID: 4441086]
5.  Spadari, S., Subramanian, A.R. and Kalnitsky, G. Highly restricted specificity of the serine proteinase aspergillopeptidase B. Biochim. Biophys. Acta 359 (1974) 267–272. [DOI] [PMID: 4859351]
[EC created 1992 (EC created 1961 as EC, transferred 1972 to EC, modified 1986, part incorporated 1992)]

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