Protease from Bacillus cereus ATCC 4342

Enzyme Description

Extremophile
No
EC Number

Sequence

Length: 316 amino acids
VTGTNKVGTGKGVLGDTKSLNTTLSGSSYYLQDNTRGATIFTYDAKNRSTLPGTLWADADNVFNAAYDAAAVDAHYYAGKTYDYYKATFNRNSINDAGAPLKSTVHYGSNYNNAFWNGSQMVYGDGDGVTFTSLSGGIDVIGHELTHAVTENSSNLIYQNESGALNEAISDIFGTLVEFYDNRNPDWEIGEDIYTPGKAGDALRSMSDPTKYGDPDHYSKRYTGSSDNGGVHTNSGIINKQAYLLANGGTHYGVTVIGIGKDKLGAIYYRANTQYFTQSTTFSQARAGAVQAAADLYGANSAEVAAVKQSFSAVGV
Tolbert Osire et al. (2019) β€” Lys–Arg mutation improved the thermostability of Bacillus cereus neutral protease through increased residue interactions
World Journal of Microbiology and Biotechnology  Β· doi:10.1007/s11274-019-2751-5 β†—  Β· Activity - Classical
7 measurements
Database ID
β€”
Sequence Annotation
Explicit - Provided (249 first residues from UniProt sequence absent from the mature protein)
Protein Source
Recombinant, host bacterium Escherichia coli BL21

Experimental Data (7 measurements)

7 measurements
Property Assay Solvent Solvent Volume Aqueous Reference Measured Value Units Solution pH Temperature Substrate(s) Product(s) Cofactor(s) Shaking Comments
Activity - Classical Activity measured by absorbance spectrophotometry (colorimetric assay, Folin-Ciocalteu phenol reactant and free tyrosines reaction product absorbance measurement, 660 nm) in the presence of organic solvent Benzene 10% 100.0 61.0 % Tris-HCl buffer 7.4 37Β°C 1% Casein free amino acids , Peptides β€” β€” Classical aqueous control (in %)
Activity - Classical Activity measured by absorbance spectrophotometry (colorimetric assay, Folin-Ciocalteu phenol reactant and free tyrosines reaction product absorbance measurement, 660 nm) in the presence of organic solvent Ethanol 10% 100.0 89.28 % Tris-HCl buffer 7.4 37Β°C 1% Casein free amino acids , Peptides β€” β€” Classical aqueous control (in %)
Activity - Classical Activity measured by absorbance spectrophotometry (colorimetric assay, Folin-Ciocalteu phenol reactant and free tyrosines reaction product absorbance measurement, 660 nm) in the presence of organic solvent Acetonitrile 10% 100.0 84.63 % Tris-HCl buffer 7.4 37Β°C 1% Casein free amino acids , Peptides β€” β€” Classical aqueous control (in %)
Activity - Classical Activity measured by absorbance spectrophotometry (colorimetric assay, Folin-Ciocalteu phenol reactant and free tyrosines reaction product absorbance measurement, 660 nm) in the presence of organic solvent Methanol 10% 100.0 94.32 % Tris-HCl buffer 7.4 37Β°C 1% Casein free amino acids , Peptides β€” β€” Classical aqueous control (in %)
Activity - Classical Activity measured by absorbance spectrophotometry (colorimetric assay, Folin-Ciocalteu phenol reactant and free tyrosines reaction product absorbance measurement, 660 nm) in the presence of organic solvent Toluene 10% 100.0 112.91 % Tris-HCl buffer 7.4 37Β°C 1% Casein free amino acids , Peptides β€” β€” Classical aqueous control (in %)
Activity - Classical Activity measured by absorbance spectrophotometry (colorimetric assay, Folin-Ciocalteu phenol reactant and free tyrosines reaction product absorbance measurement, 660 nm) in the presence of organic solvent n-Hexane 10% 100.0 91.61 % Tris-HCl buffer 7.4 37Β°C 1% Casein free amino acids , Peptides β€” β€” Classical aqueous control (in %)
Activity - Classical Activity measured by absorbance spectrophotometry (colorimetric assay, Folin-Ciocalteu phenol reactant and free tyrosines reaction product absorbance measurement, 660 nm) in the presence of organic solvent Dimethyl Sulfoxide (DMSO) 10% 100.0 94.7 % Tris-HCl buffer 7.4 37Β°C 1% Casein free amino acids , Peptides β€” β€” Classical aqueous control (in %)

Visualization : Activity β€” Classical

One bar per measurement. Colour = solvent, shade = solvent volume.

Structure

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