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EC Tree
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,
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Alkaline proteinase
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alkaline serine protease
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Aspergillopepsin B
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Aspergillopepsin F
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Aspergillopeptidase B
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Aspergillus alkaline proteinase
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Aspergillus candidus alkaline proteinase
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Aspergillus flavus alkaline proteinase
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Aspergillus melleus semi-alkaline proteinase
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Aspergillus oryzae alkaline proteinase
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Aspergillus parasiticus alkaline proteinase
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Aspergillus serine proteinase
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Elastinolytic serine proteinase
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Proteinase, Aspergillus alkaline
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Proteinase, Aspergillus flavus alkaline
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Proteinase, Aspergillus melleus alkaline
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Proteinase, Aspergillus oryzae alkaline
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Proteinase, Aspergillus parasiticus alkaline
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Proteinase, Aspergillus soya alkaline
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Proteinase, Aspergillus sulphureus alkaline
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Proteinase, Aspergillus sydowi alkaline
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Semi-alkaline protease
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hydrolysis of peptide bond
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azocasein + H2O
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?
casein + H2O
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artificial substrate
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?
casein + H2O
hydrolyzed casein
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?
Hemoglobin + H2O
Hydrolyzed hemoglobin
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L-Leu 4-nitroanilide hydrochloride + H2O
?
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?
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Fe2+
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activates 1.74fold at 5 mM
K+
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activates about 10% at 5 mM
Na+
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activates about 10% at 5 mM
additional information
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no effect on enzyme activity by 5 mM Pb2+. Effect of metal salts on enzyme production, overview
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Co2+
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about 10% inhibition at 5 mM
Cu2+
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over 90% inhibition at 5 mM
Hg2+
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complete inhibition at 5 mM
Mn2+
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about 30% inhibition at 5 mM
Ni2+
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about 20% inhibition at 5 mM
Zn2+
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about 20% inhibition at 5 mM
additional information
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EDTA
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additional information
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KCN
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additional information
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PCMB
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additional information
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not: sulfhydryl reagents
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additional information
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cysteine
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additional information
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poor inhibition by Ca2+ at 5 mM
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additional information
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additional information
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6 - 11
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small changes of activity between pH 6 and 11
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30 - 55
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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
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UniProt
brenda
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additional information
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the organism is grown under solid state fermentation. Maximum protease yield is obtained when the strain is grown under wheat bran and corn cob mixture, ratio 1:1, incubated for 48 h at pH 9.0 and temperature 37°C with 50% of initial moisture content, evaluation overview
brenda
additional information
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secreted enzyme of spores from solid-state fermentation conditions on wheat bran. All corneal isolates showed higher exoprotease activity compared to the saprophyte strain ATCC26
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brenda
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the enzyme is secreted and forms aprt of the exoproteasome
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brenda
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physiological function
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the enzyme is a virulence factor for the organism infecting the human eye cornea and causing keratitis
additional information
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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
additional information
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structure-function analysis, three-dimensional structure and comparative and homology modeling, overview
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ORYZ_ASPFL
403
1
42769
Swiss-Prot
Secretory Pathway (Reliability: 3 )
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18000
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Aspergillus flavus
22000 - 24000
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Aspergillus flavus, gel filtration
23620 - 27180
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Aspergillus flavus, ultracentrifugal measurements
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additional information
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primary and secondary enzyme structure analysis, the enzyme has 42% alpha-helix content, three-dimensional structure modeling, overview
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additional information
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Aspergillus sojae enzyme contains no sugar, Aspergillus flavus alkaline proteinase contains 1 mol ribose per mol of protein
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7 - 12
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partially purified enzyme, stable at
717055
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30 - 40
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partially purified enzyme, stable at, retention of 96% activity after 1 h of incubation at 40°C
45
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84% residual activity after 1 h of incubation at 45°C
55
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53% residual activity after 1 h of incubation at 55°C
additional information
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thermal stability profile, overview
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Acetone
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97.1% remaining activity after 1 h at 30°C in 25% organic solvent
benzene
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89.2% remaining activity after 1 h at 30°C in 25% organic solvent
Butanol
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96.2% remaining activity after 1 h at 30°C in 25% organic solvent
chloroform
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105.3% activity after 1 h at 30°C in 25% organic solvent
diethyl ether
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89.2% remaining activity after 1 h at 30°C in 25% organic solvent
Ethanol
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83.2% remaining activity after 1 h at 30°C in 25% organic solvent
hexane
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94.3% remaining activity after 1 h at 30°C in 25% organic solvent
Methanol
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81.7% remaining activity after 1 h at 30°C in 25% organic solvent
toluene
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91.7% remaining activity after 1 h at 30°C in 25% organic solvent
xylene
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83.6% remaining activity after 1 h at 30°C in 25% organic solvent
additional information
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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
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oxidant stable serine protease. The enzyme retains 100% of its original activity with 10% H2O2 after 1 h of incubation at 30°C
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717055
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native enzyme partially by acetone precipitation
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var. columnaris, partial
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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
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industry
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possible use of the enzyme in detergent industry and peptide synthesis due to its compatibility with several detergents, oxidants and organic solvents
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Nakagawa, Y.
Alkaline proteinases from Aspergillus
Methods Enzymol.
19
581-591
1970
Aspergillus flavus, Aspergillus oryzae, Aspergillus sojae, Aspergillus sydowii
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brenda
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
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Turkova, J.; Mikes, O.
Reinvestigation of molecular weight of alkaline proteinase from Aspergillus flavus
Collect. Czech. Chem. Commun.
37
1408-1411
1972
Aspergillus flavus
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brenda
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
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brenda
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)
brenda
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
brenda
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
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