Oryzin - Misplaced Pages

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. 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

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.
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.
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.
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.
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.

External links

Oryzin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

v t e Endopeptidases: serine proteases/serine endopeptidases (EC 3.4.21)
Digestive enzymes	Enteropeptidase Trypsin Chymotrypsin Elastase Neutrophil Pancreatic
Coagulation	factors: Thrombin Factor VIIa Factor IXa Factor Xa Factor XIa Factor XIIa Kallikrein PSA KLK1 KLK2 KLK3 KLK4 KLK5 KLK6 KLK7 KLK8 KLK9 KLK10 KLK11 KLK12 KLK13 KLK14 KLK15 fibrinolysis: Plasmin Plasminogen activator Tissue plasminogen activator Urinary plasminogen activator
Complement system	Factor B Factor D Factor I MASP MASP1 MASP2 C3-convertase
Other immune system	Chymase Granzyme Tryptase Proteinase 3/Myeloblastin
Venombin	Ancrod Batroxobin
Other	Acrosin Prolyl endopeptidase Pronase Proprotein convertases 1 2 Prostasin Reelin Subtilisin/Furin/S1P4 Sedolisin/TPP1 Streptokinase Cathepsin A G

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Portal:

Biology

Category:

EC 3.4.21