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

Oryzin
Identifiers
EC no.3.4.21.63
CAS no.2620433
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
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

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  1. ^ Nakagawa, Y. (1970). "Alkaline proteinases from Aspergillus". Alkaline proteinases from Aspergillus. Methods Enzymol. Vol. 19. pp. 581–591. doi:10.1016/0076-6879(70)19046-x. ISBN 978-0-12-181881-4.
  2. ^ Hayashi, K.; Terada, M. (1972). "Some characteristics of hydrolysis of synthetic substrates and proteins by the alkaline proteases from Aspergillus sojae". Agric. Biol. Chem. 36 (10): 1755–1765. doi:10.1271/bbb1961.36.1755.
  3. ^ Turkovã J, Mikes O, Hayashi K, Danno G, Polgãr L (February 1972). "Alkaline proteinases of the genus Aspergillus". Biochimica et Biophysica Acta (BBA) - Protein Structure. 257 (2): 257–63. doi:10.1016/0005-2795(72)90277-2. PMID 4623338.
  4. ^ Morihara K, Oka T, Tsuzuki H (November 1974). "Comparative study of various serine alkaline proteinases from microorganisms. Esterase activity against N-acylated peptide ester substrates". Archives of Biochemistry and Biophysics. 165 (1): 72–9. doi:10.1016/0003-9861(74)90143-x. PMID 4441086.
  5. ^ Spadari S, Subramanian AR, Kalnitsky G (August 1974). "Highly restricted specificity of the serine proteinase aspergillopeptidase B". Biochimica et Biophysica Acta (BBA) - Protein Structure. 359 (2): 267–72. doi:10.1016/0005-2795(74)90224-4. PMID 4859351.
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