3.4.21.63: Oryzin
This is an abbreviated version!
For detailed information about Oryzin, go to the full flat file.
Word Map on EC 3.4.21.63
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3.4.21.63
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neutrophil
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leukocyte
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pancreatic
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pulmonary
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aeruginosa
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polymorphonuclear
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cathepsin
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chymotrypsin
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emphysema
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collagenase
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porcine
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arterial
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granulocyte
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myeloperoxidase
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proteinases
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lavage
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aortic
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elastolytic
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alveolar
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airway
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aneurysm
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elastic
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instil
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thrombin
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intratracheal
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bronchoalveolar
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cystic
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plasmin
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degranulation
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lactoferrin
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antiprotease
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fmlp
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alpha-1-antitrypsin
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azurophilic
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exocrine
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serpins
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quorum
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1-antitrypsin
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pyocyanin
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2-macroglobulin
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sputum
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subtilisin
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hne
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crevicular
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detergent
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wegener
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ancas
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industry
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neutrophil-derived
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food industry
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nutrition
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neutrophil-mediated
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slpi
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anti-neutrophil
- 3.4.21.63
- neutrophil
- leukocyte
- pancreatic
- pulmonary
- aeruginosa
-
polymorphonuclear
- cathepsin
- chymotrypsin
- emphysema
- collagenase
- porcine
- arterial
- granulocyte
- myeloperoxidase
- proteinases
-
lavage
- aortic
-
elastolytic
- alveolar
- airway
- aneurysm
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elastic
-
instil
- thrombin
-
intratracheal
-
bronchoalveolar
-
cystic
- plasmin
-
degranulation
- lactoferrin
-
antiprotease
- fmlp
- alpha-1-antitrypsin
-
azurophilic
-
exocrine
- serpins
-
quorum
-
1-antitrypsin
- pyocyanin
-
2-macroglobulin
- sputum
- subtilisin
- hne
-
crevicular
- detergent
-
wegener
-
ancas
- industry
-
neutrophil-derived
- food industry
- nutrition
-
neutrophil-mediated
- slpi
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anti-neutrophil
Reaction
Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt > Ac-Tyr-OEt. Does not hydrolyse peptide amides =
Synonyms
Alkaline protease, Alkaline proteinase, alkaline serine protease, ALP, ALP1, AOP, AP15, AP30, API 21, Aspergillopepsin B, Aspergillopepsin F, Aspergillopeptidase B, Aspergillus alkaline proteinase, Aspergillus candidus alkaline proteinase, Aspergillus flavus alkaline proteinase, Aspergillus melleus semi-alkaline proteinase, Aspergillus oryzae alkaline proteinase, Aspergillus oryzae protease, Aspergillus parasiticus alkaline proteinase, Aspergillus serine proteinase, Aspergillus terreus protease, collagenolytic serine peptidase, EC 3.4.21.14, EC 3.4.21.15, EC 3.4.4.16, elastase, Elastinolytic serine proteinase, Kyorinase, neutral protease I, NpI, Onoprose, Onoprose SA, P 5380, Promelase, protease Alp1, Protease P, Proteinase, Aspergillus alkaline, Proteinase, Aspergillus flavus alkaline, Proteinase, Aspergillus melleus alkaline, Proteinase, Aspergillus oryzae alkaline, Proteinase, Aspergillus parasiticus alkaline, Proteinase, Aspergillus soya alkaline, Proteinase, Aspergillus sulphureus alkaline, Proteinase, Aspergillus sydowi alkaline, Prozyme, Prozyme 10, PrtA, PrtA protease, SapHM, Seaprose S, Semi-alkaline protease, Sumizyme MP
ECTree
3.4.21.63 OryzinAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.21.63 - Oryzin
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-phenyllactic acid + H2O
?
-
methyl esters and its ring-substituted derivative hydrolyzed with excellent enantioselectivities
-
-
?
Ile-Gln-Asn-Cys-Pro-Leu-Gly-NH2 + H2O
Ile-Gln-Asn-Cys-Pro-Leu + Gly-NH2
-
-
-
?
N-Acetyl amino acid ester + H2O
?
-
hydrolysis decreases in the order of Phe/ Tyr, Trp, Met, Leu, Lys, His, Val/ Gly
-
-
?
N-Cbz-L-Tyr + 1-phenylethanol
N-Cbz-L-Tyr-1-phenylethyl ester
-
-
-
?
Oxidized insulin A-chain + H2O
Hydrolyzed oxidized insulin A-chain
-
at 0øC the enzyme cleaves only the bond Glu17-Asn18
-
-
?
Oxidized insulin B-chain + H2O
?
-
eight cleavage sites of the enzyme in oxidized insulin B-chain are determined by mass spectrometry, and five of them have high hydrophobic amino acid affinity
-
-
?
Acetyl-Ala-Ala-Ala methyl ester + H2O
Acetyl-Ala-Ala-Ala + methanol
-
-
-
-
?
Acetyl-Ala-Ala-Ala methyl ester + H2O
Acetyl-Ala-Ala-Ala + methanol
-
-
-
-
?
Acetyl-Ala-Ala-Ala methyl ester + H2O
Acetyl-Ala-Ala-Ala + methanol
-
-
-
-
?
Acetyl-Ala-Ala-Ala-Ala methyl ester + H2O
Acetyl-Ala-Ala-Ala-Ala + methanol
-
-
-
-
?
Acetyl-Ala-Ala-Ala-Ala methyl ester + H2O
Acetyl-Ala-Ala-Ala-Ala + methanol
-
-
-
-
?
Acetyl-Ala-Ala-Phe methyl ester + H2O
Acetyl-Ala-Ala-Phe + methanol
-
-
-
-
?
Acetyl-Ala-Ala-Phe methyl ester + H2O
Acetyl-Ala-Ala-Phe + methanol
-
-
-
-
?
Ala-Ala-Pro-Arg-4-nitroanilide + H2O
Ala-Ala-Pro-Arg + 4-nitroaniline
very low activity of 3.3% compared to Ala-Ala-Pro-Phe-4-nitroanilide
-
-
?
Ala-Ala-Pro-Arg-4-nitroanilide + H2O
Ala-Ala-Pro-Arg + 4-nitroaniline
Aspergillus sojae GIM3.33
very low activity of 3.3% compared to Ala-Ala-Pro-Phe-4-nitroanilide
-
-
?
Ala-Ala-Pro-Asn-4-nitroanilide + H2O
Ala-Ala-Pro-Asn + 4-nitroaniline
very low activity of 1.1% compared to Ala-Ala-Pro-Phe-4-nitroanilide
-
-
?
Ala-Ala-Pro-Asn-4-nitroanilide + H2O
Ala-Ala-Pro-Asn + 4-nitroaniline
Aspergillus sojae GIM3.33
very low activity of 1.1% compared to Ala-Ala-Pro-Phe-4-nitroanilide
-
-
?
Ala-Ala-Pro-Phe-4-nitroanilide + H2O
Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
Ala-Ala-Pro-Phe-4-nitroanilide + H2O
Ala-Ala-Pro-Phe + 4-nitroaniline
Aspergillus sojae GIM3.33
-
-
-
?
Benzyloxycarbonyl-Ala-Ala-Lys methyl ester + H2O
Benzyloxycarbonyl-Ala-Ala-Lys + methanol
-
-
-
-
?
Benzyloxycarbonyl-Ala-Ala-Lys methyl ester + H2O
Benzyloxycarbonyl-Ala-Ala-Lys + methanol
-
-
-
-
?
Benzyloxycarbonyl-Ala-Lys methyl ester + H2O
Benzyloxycarbonyl-Ala-Lys + methanol
-
-
-
-
?
Benzyloxycarbonyl-Ala-Lys methyl ester + H2O
Benzyloxycarbonyl-Ala-Lys + methanol
-
-
-
-
?
Benzyloxycarbonyl-Gly-Lys methyl ester + H2O
Benzyloxycarbonyl-Gly-Lys + methanol
-
-
-
-
?
Benzyloxycarbonyl-Gly-Lys methyl ester + H2O
Benzyloxycarbonyl-Gly-Lys + methanol
-
-
-
-
?
Benzyloxycarbonyl-Leu-Lys methyl ester + H2O
Benzyloxycarbonyl-Leu-Lys + methanol
-
-
-
-
?
Benzyloxycarbonyl-Leu-Lys methyl ester + H2O
Benzyloxycarbonyl-Leu-Lys + methanol
-
-
-
-
?
Benzyloxycarbonyl-Lys methyl ester + H2O
Benzyloxycarbonyl-Lys + methanol
-
-
-
-
?
Benzyloxycarbonyl-Lys methyl ester + H2O
Benzyloxycarbonyl-Lys + methanol
-
-
-
-
?
Benzyloxycarbonyl-Phe-Lys methyl ester + H2O
Benzyloxycarbonyl-Phe-Lys + methanol
-
-
-
-
?
Benzyloxycarbonyl-Phe-Lys methyl ester + H2O
Benzyloxycarbonyl-Phe-Lys + methanol
-
-
-
-
?
Bovine serum albumin + H2O
?
-
18% activity compared to casein
-
-
?
casein + H2O
?
-
the enzyme has a high affinity for the casein, best substrate
-
-
?
casein + H2O
?
-
the enzyme has a high affinity for the casein, best substrate
-
-
?
casein + H2O
hydrolyzed casein
-
active centre of the enzyme contains serine residues
-
-
?
casein + H2O
hydrolyzed casein
-
active centre of the enzyme contains serine residues
-
-
?
defatted soybean complex medium + H2O
?
-
increase in production by adding lactose, casitone or casein, even glucose, starch, sucrose, maltose, or arabinose
-
?
defatted soybean complex medium + H2O
?
-
increase in production by adding lactose, casitone or casein, even glucose, starch, sucrose, maltose, or arabinose
-
?
Gelatin + H2O
?
-
the active enzyme degrades the copolymerized gelatin with high activity
-
-
?
Gelatin + H2O
?
-
the active enzyme degrades the copolymerized gelatin with high activity
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
-
at 0øC the enzyme cleaves only the bond Leu15-Tyr16
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
-
-
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
-
-
-
-
?
additional information
?
-
the enzyme performs well in removing an egg protein stain when supplemented into a commercial powder detergent
-
-
?
additional information
?
-
Aspergillus fischeri ATCC 1020
the enzyme performs well in removing an egg protein stain when supplemented into a commercial powder detergent
-
-
?
additional information
?
-
the enzyme performs well in removing an egg protein stain when supplemented into a commercial powder detergent
-
-
?
additional information
?
-
Aspergillus fischeri DSM 3700
the enzyme performs well in removing an egg protein stain when supplemented into a commercial powder detergent
-
-
?
additional information
?
-
Aspergillus fischeri FGSC A1164
the enzyme performs well in removing an egg protein stain when supplemented into a commercial powder detergent
-
-
?
additional information
?
-
Aspergillus fischeri JCM 1740
the enzyme performs well in removing an egg protein stain when supplemented into a commercial powder detergent
-
-
?
additional information
?
-
Aspergillus fischeri WB 181
the enzyme performs well in removing an egg protein stain when supplemented into a commercial powder detergent
-
-
?
additional information
?
-
-
secreted Aspergillus fumigatus protease Alp1 degrades human complement proteins in culture supernatant C3, C4, C5, and C1q as well as immunoglobulin G. C4 is completely degraded. Degradation of C5 and C1q is also observed but is less prominent
-
-
?
additional information
?
-
-
secreted Aspergillus fumigatus protease Alp1 degrades human complement proteins in culture supernatant C3, C4, C5, and C1q as well as immunoglobulin G. C4 is completely degraded. Degradation of C5 and C1q is also observed but is less prominent
-
-
?
additional information
?
-
-
the esterase activity is markedly promoted by elongating the peptide chain from P1 to P2 or P3 with alanine, irrespectively of the kind of the amino acid residue at the P1-position
-
-
?
additional information
?
-
-
leucine or phenylalanine is most efficient at the P2-position
-
-
?
additional information
?
-
-
action of Aspergillus oryzae protease on whey proteins, analysis of the enzymatic hydrolysates, method evaluation and peptide profile determined by size exclusion HPLC, overview. The enzyme shows a strong negative correlation between the large peptide content and the degree of hydrolysis
-
-
?
additional information
?
-
-
the enzyme shows a high degree of hydrolysis with soybean protein (8.8%) and peanut protein (11.1%) compared to papain and alcalase
-
-
?
additional information
?
-
-
the esterase activity is markedly promoted by elongating the peptide chain from P1 to P2 or P3 with alanine, irrespectively of the kind of the amino acid residue at the P1-position
-
-
?
additional information
?
-
-
in the hydrolysis of natural proteins, the enzyme liberates relatively large peptides and traces (endo-type)
-
-
?
additional information
?
-
-
leucine or phenylalanine is most efficient at the P2-position
-
-
?
additional information
?
-
-
relatively high specificity for lysine, tyrosine, histidine, arginine and phenylalanine residues
-
-
?
additional information
?
-
the recombinan enzyme shows a broad substrate specificity for natural proteins (e.g. soy proteins) and synthetic peptide substrates, and prefers substrates at P1 position with large hydrophobic side-chain groups. Ala-Ala-Pro-Glu-4-nitroanilide and glutin are a poor substrate
-
-
?
additional information
?
-
Aspergillus sojae GIM3.33
the recombinan enzyme shows a broad substrate specificity for natural proteins (e.g. soy proteins) and synthetic peptide substrates, and prefers substrates at P1 position with large hydrophobic side-chain groups. Ala-Ala-Pro-Glu-4-nitroanilide and glutin are a poor substrate
-
-
?
additional information
?
-
the enzyme performs well in removing an egg protein stain when supplemented into a commercial powder detergent
-
-
?
