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Information on EC 3.4.21.63 - Oryzin and Organism(s) Aspergillus flavus and UniProt Accession P35211

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.63 Oryzin
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Aspergillus flavus
UNIPROT: P35211 not found.
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The taxonomic range for the selected organisms is: Aspergillus flavus
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Alkaline protease
-
-
Alkaline proteinase
-
-
-
-
alkaline serine protease
-
-
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 hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9074-07-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
azocasein + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
-
artificial substrate
-
-
?
casein + H2O
hydrolyzed casein
show the reaction diagram
-
-
-
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
show the reaction diagram
-
-
-
-
?
L-Leu 4-nitroanilide hydrochloride + H2O
?
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
activates 1.74fold at 5 mM
K+
-
activates about 10% at 5 mM
Na+
-
activates about 10% at 5 mM
additional information
-
no effect on enzyme activity by 5 mM Pb2+. Effect of metal salts on enzyme production, overview
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Co2+
-
about 10% inhibition at 5 mM
Cu2+
-
over 90% inhibition at 5 mM
Hg2+
-
complete inhibition at 5 mM
Mn2+
-
about 30% inhibition at 5 mM
N-bromosuccinimide
-
-
Ni2+
-
about 20% inhibition at 5 mM
Zn2+
-
about 20% inhibition at 5 mM
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 11
-
small changes of activity between pH 6 and 11
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
50 - 55
-
casein
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 55
-
100% activity at 40°C while 92% residual activity at 45°C, 74% at 50°C, and 41% 55°C, inactive above 55°C, temperature profile, overview
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
the enzyme is a virulence factor for the organism infecting the human eye cornea and causing keratitis
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ORYZ_ASPFL
403
1
42769
Swiss-Prot
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18000
-
Aspergillus flavus
22000 - 24000
-
Aspergillus flavus, gel filtration
23620 - 27180
-
Aspergillus flavus, ultracentrifugal measurements
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
primary and secondary enzyme structure analysis, the enzyme has 42% alpha-helix content, three-dimensional structure modeling, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
Aspergillus sojae enzyme contains no sugar, Aspergillus flavus alkaline proteinase contains 1 mol ribose per mol of protein
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 12
-
partially purified enzyme, stable at
717055
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 40
-
partially purified enzyme, stable at, retention of 96% activity after 1 h of incubation at 40°C
45
-
84% residual activity after 1 h of incubation at 45°C
55
-
53% residual activity after 1 h of incubation at 55°C
additional information
-
thermal stability profile, overview
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acetone
-
97.1% remaining activity after 1 h at 30°C in 25% organic solvent
benzene
-
89.2% remaining activity after 1 h at 30°C in 25% organic solvent
Butanol
-
96.2% remaining activity after 1 h at 30°C in 25% organic solvent
chloroform
-
105.3% activity after 1 h at 30°C in 25% organic solvent
diethyl ether
-
89.2% remaining activity after 1 h at 30°C in 25% organic solvent
Ethanol
-
83.2% remaining activity after 1 h at 30°C in 25% organic solvent
hexane
-
94.3% remaining activity after 1 h at 30°C in 25% organic solvent
Methanol
-
81.7% remaining activity after 1 h at 30°C in 25% organic solvent
toluene
-
91.7% remaining activity after 1 h at 30°C in 25% organic solvent
xylene
-
83.6% remaining activity after 1 h at 30°C in 25% organic solvent
additional information
-
extremely organic solvent stable serine protease. The enzyme retains 80% of its original activity in the presence of non ionic and ionic surfactants after 1 h of incubation at 30°C, overview
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxidant stable serine protease. The enzyme retains 100% of its original activity with 10% H2O2 after 1 h of incubation at 30°C
-
717055
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme partially by acetone precipitation
-
var. columnaris, partial
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
sequence comparisons between Aspergillus species and different proteases, clustering of alkaline proteases, phylogenetic tree, overview
sequence comparisons between Aspergillus species and different proteases, clustering of alkaline proteases, phylogenetic tree, overview
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
industry
-
possible use of the enzyme in detergent industry and peptide synthesis due to its compatibility with several detergents, oxidants and organic solvents
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nakagawa, Y.
Alkaline proteinases from Aspergillus
Methods Enzymol.
19
581-591
1970
Aspergillus flavus, Aspergillus oryzae, Aspergillus sojae, Aspergillus sydowii
-
Manually annotated by BRENDA team
Impoolsup, A.; Bhumiratana, A.; Flegel, T.W.
Isolation of alkaline and neutral proteases from Aspergillus flavus var. columnaris, a soy sauce koji mold
Appl. Environ. Microbiol.
42
619-628
1981
Aspergillus flavus
Manually annotated by BRENDA team
Turkova, J.; Mikes, O.
Reinvestigation of molecular weight of alkaline proteinase from Aspergillus flavus
Collect. Czech. Chem. Commun.
37
1408-1411
1972
Aspergillus flavus
-
Manually annotated by BRENDA team
Yadav, S.; Bisht, D.; Shikh, S.; Darmwal, N.
Oxidant and solvent stable alkaline protease from Aspergillus flavus and its characterization
Afr. J. Biotechnol.
10
8630-8640
2011
Aspergillus flavus, Aspergillus flavus MTCC 9952
-
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Syed, R.; Rani, R.; Sabeena, R.; Masoodi, T.A.; Shafi, G.; Alharbi, K.
Functional analysis and structure determination of alkaline protease from Aspergillus flavus
Bioinformation
8
175-180
2012
Aspergillus flavus
Manually annotated by BRENDA team
Selvam, R.M.; Nithya, R.; Devi, P.N.; Shree, R.S.; Nila, M.V.; Demonte, N.L.; Thangavel, C.; Maheshwari, J.J.; Lalitha, P.; Prajna, N.V.; Dharmalingam, K.
Exoproteome of Aspergillus flavus corneal isolates and saprophytes: Identification of proteoforms of an oversecreted alkaline protease
J. Proteomics
115
23-35
2015
Aspergillus flavus
Manually annotated by BRENDA team