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Oryzin

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Oryzin
Identifiers
EC no.3.4.21.63
CAS no.2620433
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
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NCBIproteins

Oryzin (EC 3.4.21.63, 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) is an enzyme.[1][2][3][4][5] This enzyme catalyses the following chemical reaction

Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt > Ac-Tyr-OEt. Does not hydrolyse peptide amides

This enzyme is a predominant extracellular alkaline endopeptidase of the mold Aspergillus oryzae.

References

  1. ^ Nakagawa, Y. (1970). "Alkaline proteinases from Aspergillus". Methods Enzymol. 19: 581–591. doi:10.1016/0076-6879(70)19046-x.
  2. ^ Hayashi, K. and Terada, M. (1972). "Some characteristics of hydrolysis of synthetic substrates and proteins by the alkaline proteases from Aspergillus sojae". Agric. Biol. Chem. 36: 1755–1765. doi:10.1271/bbb1961.36.1755.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  3. ^ Turková, J., Mikes, O., Hayashi, K., Danno, G. and Polgár, L. (1972). "Alkaline proteinases of the genus Aspergillus". Biochim. Biophys. Acta. 257: 257–263. doi:10.1016/0005-2795(72)90277-2. PMID 4623338.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  4. ^ Morihara, K., Oka, T. and Tsuzuki, H. (1974). "Comparative study of various serine alkaline proteinases from microorganisms. Esterase activity against N-acylated peptide ester substrates". Arch. Biochem. Biophys. 165: 72–79. doi:10.1016/0003-9861(74)90143-x. PMID 4441086.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  5. ^ Spadari, S., Subramanian, A.R. and Kalnitsky, G. (1974). "Highly restricted specificity of the serine proteinase aspergillopeptidase B". Biochim. Biophys. Acta. 359: 267–272. doi:10.1016/0005-2795(74)90224-4. PMID 4859351.{{cite journal}}: CS1 maint: multiple names: authors list (link)