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Information on EC 3.4.21.63 - Oryzin and Organism(s) Aspergillus oryzae and UniProt Accession P12547
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3.4.21.63 OryzinSpecify your search results
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- 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
-
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
-
anti-neutrophil
The taxonomic range for the selected organisms is: Aspergillus oryzae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
elastase, alkaline proteinase, prozyme, protease p, seaprose s, aspergillus oryzae protease, aspergillopepsin b, oryzin, protease alp1, neutral protease i, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Alkaline proteinase
-
-
-
-
ALP
-
-
-
-
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 parasiticus alkaline proteinase
-
-
-
-
Aspergillus serine proteinase
-
-
-
-
elastase
-
-
-
-
Elastinolytic serine proteinase
-
-
-
-
Kyorinase
-
-
-
-
Onoprose
-
-
-
-
Onoprose SA
-
-
-
-
P 5380
-
-
-
-
Promelase
-
-
-
-
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
-
-
-
-
Seaprose S
-
-
-
-
Semi-alkaline protease
-
-
-
-
Sumizyme MP
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9074-07-1
-
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
-
-
?
Acetyl-Ala-Ala-Ala methyl ester + H2O
Acetyl-Ala-Ala-Ala + methanol
-
-
-
-
?
defatted soybean complex medium + H2O
?
-
increase in production by adding lactose, casitone or casein, even glucose, starch, sucrose, maltose, or arabinose
-
?
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
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
-
at 0øC the enzyme cleaves only the bond Leu15-Tyr16
-
-
?
casein + H2O
hydrolyzed casein
-
active centre of the enzyme contains serine residues
-
-
?
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
NaCl
-
over 20% relative activity of the enzyme remains in the presence of 3.0 mo/l NaCl after 7 days, but its Km and Vmax are only mildly influenced. The salt-tolerant mechanisms of the enzyme might be due to more salt bridges, higher proportion of ordered secondary structures and stronger hydrophobic amino acid residues in the interior
additional information
additional information
-
no significant effect with Mn2+ and Cu2+ at 2-5 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-tosyl-L-lysine chloromethyl ketone
inhibitor of recombinant and native enzyme
phenylmethylsulfonyl fluoride
strong inhibitor of recombinant and native enzyme
4-nitrophenyl acetate
-
increasing concentrations of the ester inhibit casein hydrolysis
additional information
-
not inhibited by Cu2+, Sn2+, Ba2+, Co2+, Li+, benzamidine, beta-ME, cysteine, EDTA and 1,10-phenathroline
-
additional information
-
no or poor effect by 5 mM of EDTA, o-phenanthroline, bestatin, or 1 mM Zn2+
-
additional information
-
Triton X-100 and PMSF have no inhibitory effect on the enzyme activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
during growth on solid cereal substrates, protease activity in extracts of hemoglobin domain-activity-producing strains is 30-150% higher compared to the wild-type strain
-
additional information
-
stabilization of the enzyme in entrapped Ca-alginate beads, activity maximal (ca. 48%) at 2% (w/v) sodium alginate concentration
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
additional information
additional information
-
Km for the immobilized enzyme is 1.5fold higher than for the free enzyme
-
additional information
additional information
-
casein gives a Vmax of 141.1 ng/min and a Km of 2432 ng/ml
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
584000 U/g, one unit is the amount of enzyme that produces TCA mixture-soluble materials equivalent to 1 microgram of tyrosine from casein per min at pH 9.0 and 45°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
cultivation on solid medium, optimization of culture conditions, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enzyme produced in shake cultures is secreted in the stationary phase when cells are grown on nutrient broth, and in early growth on defined salts
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme structure homology modeling. The active center of the alkaline protease is established by three amino acid residues Asp41, His72, and Ser228, based on the result of protein sequence alignment between the alkaline protease and cuticle-degrading protease from north american fungi, three-dimensional structures, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme disruption mutant, strain shows much more compact colony morphology than wild-type. Sporulation occurs two days later, and hyphal growth and length is on average 50% of that of wild-type, with increased hyphal branching. After growth on wheat kernels, mutant strain produces at least 50% higher amylase, 100% higher glucoamylase and 90% higher protease activity levels than wild-type
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 10
-
immobilized enzyme, shows enhanced stability in acidic as well as alkaline environments in comparison to the free enzyme (stable between pH 7.0-9.0)
680260
7 - 11
-
purified enzyme, over 60% activity remaining, maximally stable at pH 9.0, profile overview
754496
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
55
additional information
the native enzyme exhibits a better thermostability than the recombinant enzyme
50
-
purified recombinant truncated neutral protease I, 120 min, over 90% activity remaining
55
-
immobilized enzyme retains 86% of its activity while the free enzyme retains only 10%
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by ammonium sulfate precipitation, ion exchange chromatography and gel filtration
native enzyme 1.32fold by ammonium sulfate fractionation, and anion exchange chromatography
-
native salt-tolerant alkaline protease 28fold from Aspergllus oryzae strain 3.042 by ammonium sulfate fractionation, cation exchange chromatography, and gel filtration
-
partially purified by ion exchange chromatography and gel filtration, 30fold
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
high-level expression of plasmids pPIC9K-n/Alp and pPIC9K-alpha/Alp in Pichia pastoris GS115 with native signal peptide or alpha-factor secretion signal peptide
sequence comparisons between Aspergillus species and different proteases, clustering of alkaline proteases, phylogenetic tree, overview
recombinant expression of a truncated neutral protease I in Pichia pastoris with a high enzyme yield
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
industry
-
immobilization of the enzyme as an important biotechnological aspect
nutrition
-
used in food processing, strain U1521 assumes industrial and economic importance
food industry
-
the enzyme is efficient in producing antihypertensive peptide IPP from beta-casein and a potential debittering agent. The high degree of hydrolysis of the enzyme to soybean protein (8.8%) and peanut protein (11.1%) compared to papain and alcalase makes it a good candidate in the processing of oil industry byproducts
food industry
-
the salt tolerance of proteases secreted by Aspergillus oryzae 3.042 closely relates to the utilization of raw materials and the quality of soy sauce
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Turkova, J.; Mikes, O.; Hayashi, K.; Danno, G.; Polgar, L.
Alkaline proteinases of the genus Aspergillus
Biochim. Biophys. Acta
257
257-263
1972
Aspergillus oryzae, Aspergillus sojae, Aspergillus sulphureus
Spadari, S.; Subramanian, A.R.; Kalnitsky, G.
Highly restricted specificity of the serine proteinase aspergillopeptidase B
Biochim. Biophys. Acta
359
267-272
1974
Aspergillus oryzae
Nakagawa, Y.
Alkaline proteinases from Aspergillus
Methods Enzymol.
19
581-591
1970
Aspergillus flavus, Aspergillus oryzae, Aspergillus sojae, Aspergillus sydowii
-
Nakadai, T.; Nasuno, S.; Iguchi, N.
Purification and properties of alkaline proteinase from Aspergillus oryzae
Agric. Biol. Chem.
37
2685-2694
1973
Aspergillus oryzae
-
Kundu, A.K.; Manna, S.
Purification and characterization of extracellular proteinases of Aspergillus oryzae
Appl. Microbiol.
30
507-513
1975
Aspergillus oryzae, Aspergillus oryzae EI212
Feinstein, G.; Gertler, A.
Isolation of alkaline proteinases from Aspergillus oryzae by one-step affinity chromatography on ovoinhibitor-sepharose column
Biochim. Biophys. Acta
309
196-202
1973
Aspergillus oryzae
Klapper, B.F.; Jameson, D.M.; Mayer, R.M.
The purification and properties of an extracellular protease from Aspergillus oryzae NRRL 2160
Biochim. Biophys. Acta
304
505-512
1973
Aspergillus oryzae, Aspergillus oryzae NRRL 2160
Ku, H.C.; Wyborny, L.; Kalnitsky, G.
Alkaline protease from Aspergillus oryzae: esterase activity
Biochim. Biophys. Acta
268
225-232
1972
Aspergillus oryzae
Shih, I.L.; Chiu, L.C.; Lai, C.T.; Liaw, W.C.; Tai, D.F.
Enzymes catalyzed esterification of N-protcted amino acids with secondary alcohol
Biotechnol. Lett.
19
857-859
1997
Aspergillus oryzae
-
Samarntarn, W.; Cheevadhanarak, S.; Tanticharoen, M.
Production of alkaline protease by a genetically engineered Aspergillus oryzae U1521
J. Gen. Appl. Microbiol.
45
99-103
1999
Aspergillus oryzae, Aspergillus oryzae U152
te Biesebeke, R.; Record, E.; van Biezen, N.; Heerikhuisen, M.; Franken, A.; Punt, P.J.; van den Hondel, C.A.
Branching mutants of Aspergillus oryzae with improved amylase and protease production on solid substrates
Appl. Microbiol. Biotechnol.
69
44-50
2005
Aspergillus oryzae
Miyazawa, T.; Imagawa, K.; Yamada, T.
Use of Aspergillus oryzae protease for the resolution of alpha-hydroxy acids by enantioselective ester hydrolysis
Biocatal. Biotransform.
24
291-298
2006
Aspergillus oryzae
-
te Biesebeke, R.; Boussier, A.; van Biezen, N.; Braaksma, M.; van den Hondel, C.A.; de Vos, W.M.; Punt, P.J.
Expression of Aspergillus hemoglobin domain activities in Aspergillus oryzae grown on solid substrates improves growth rate and enzyme production
Biotechnol. J.
1
822-827
2006
Aspergillus oryzae, Aspergillus oryzae ATCC 16168
Sharma, J.; Singh, A.; Kumar, R.; Mittal, A.
Partial purification of an alkaline protease from a new strain of Aspergillus oryzae AWT 20 and its enhanced stabilization in entrapped Ca-alginate beads
Internet J. Microbiol.
2
0000
2006
Aspergillus oryzae, Aspergillus oryzae AWT20
-
Guo, J.P.; Ma, Y.
High-level expression, purification and characterization of recombinant Aspergillus oryzae alkaline protease in Pichia pastoris
Protein Expr. Purif.
58
301-308
2008
Aspergillus oryzae (P12547), Aspergillus oryzae RIB 40 (P12547)
Morya, V.; Yadav, S.; Kim, E.; Yadav, D.
In silico characterization of alkaline proteases from different species of Aspergillus
Appl. Biochem. Biotechnol.
166
243-257
2012
Aspergillus clavatus (A1CIA7), Aspergillus clavatus, Aspergillus flavus (B8N106), Aspergillus flavus (P35211), Aspergillus oryzae (P12547), Aspergillus oryzae, Aspergillus flavus ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167 (B8N106), Aspergillus clavatus ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 (A1CIA7), Aspergillus oryzae RIB 40 (P12547)
Morais, H.; Silvestre, M.; Silveira, J.; Silva, A.; Silva, V.; Silva, M.
Action of a pancreatin and an Aspergillus oryzae protease on whey proteins: correlation among the methods of analysis of the enzymatic hydrolysates
Braz. Arch. Biol. Technol.
56
985-995
2013
Aspergillus oryzae
-
Ke, Y.; Huang, W.Q.; Li, J.Z.; Xie, M.Q.; Luo, X.C.
Enzymatic characteristics of a recombinant neutral protease I (rNpI) from Aspergillus oryzae expressed in Pichia pastoris
J. Agric. Food Chem.
60
12164-12169
2012
Aspergillus oryzae
Salihi, A.; Asoodeh, A.; Aliabadian, M.
Production and biochemical characterization of an alkaline protease from Aspergillus oryzae CH93
Int. J. Biol. Macromol.
94
827-835
2017
Aspergillus oryzae, Aspergillus oryzae CH93
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