Cysteine endopeptidase EP-B 2-like from Zea mays

Enzyme Description

Extremophile
No
EC Number

Sequence

Length: 368 amino acids
MAQVAKTLLLVALVVVSAVELCRAIEFDERDLASDEALWDLYERWQTHHRVHRHHGEKGRRFGTFKENARFIHAHNKRGDRPYRLRLNRFGDMGREEFRSGFADSRINDLRREPTAAPAVPGFMYDDATDLPRSVDWRQKGAVTAVKNQGRCGSCWAFSTVVAVEGINAIRTGSLVSLSEQELIDCDTDENGCQGGLMENAFEFIKSHGGITTESAYPYHASNGTCDGARARRGRVVAIDGHQAVPAGSEDALAKAVAHQPVSVAIDAGGQALQFYSEGVFTGDCGTDLDHGVAAVGYGVSDDGTPYWIVKNSWGPSWGEGGYIRMQRGTGNGGLCGIAMEASFPIKTSPNPSRKPRRALITRDASSQ
Wenjing Zhang et al. (2020) β€” Characterization of a recombinant zein-degrading protease from Zea mays by Pichia pastoris and its effects on enzymatic hydrolysis of corn starch
International Journal of Biological Macromolecules  Β· doi:10.1016/j.ijbiomac.2020.08.237 β†—  Β· Activity - Classical
8 measurements
Database ID
Sequence Annotation
Explicit - Provided GenBank Accession Number
Protein Source
Recombinant, host yeast Pichia pastoris X33

Experimental Data (8 measurements)

8 measurements
Property Assay Solvent Solvent Volume Aqueous Reference Measured Value Units Extraction method Data type Solution pH Temperature Substrate(s) Product(s) Cofactor(s) Shaking Comments
Activity - Classical Activity measured by absorbance spectrophotometry (colorimetric assay, azo-peptide absorbance measurement, 340 nm) in the presence of organic solvent Ethanol 15 % v/v 100 17 % Digital Continuous 100 mM citrate -Na2HPO4 buffer 5 40Β°C 2.5 mg/ml Azocasein Azo-peptides , Peptides β€” β€” Classical aqueous control (in %)
Activity - Classical Activity measured by absorbance spectrophotometry (colorimetric assay, azo-peptide absorbance measurement, 340 nm) in the presence of organic solvent Ethanol 30 % v/v 100 5 % Digital Continuous 100 mM citrate -Na2HPO4 buffer 5 40Β°C 2.5 mg/ml Azocasein Azo-peptides , Peptides β€” β€” Classical aqueous control (in %)
Activity - Classical Activity measured by absorbance spectrophotometry (colorimetric assay, azo-peptide absorbance measurement, 340 nm) in the presence of organic solvent Methanol 15 % v/v 100 46 % Digital Continuous 100 mM citrate -Na2HPO4 buffer 5 40Β°C 2.5 mg/ml Azocasein Azo-peptides , Peptides β€” β€” Classical aqueous control (in %)
Activity - Classical Activity measured by absorbance spectrophotometry (colorimetric assay, azo-peptide absorbance measurement, 340 nm) in the presence of organic solvent Methanol 30 % v/v 100 16 % Digital Continuous 100 mM citrate -Na2HPO4 buffer 5 40Β°C 2.5 mg/ml Azocasein Azo-peptides , Peptides β€” β€” Classical aqueous control (in %)
Activity - Classical Activity measured by absorbance spectrophotometry (colorimetric assay, azo-peptide absorbance measurement, 340 nm) in the presence of organic solvent Acetone 15 % v/v 100 33 % Digital Continuous 100 mM citrate -Na2HPO4 buffer 5 40Β°C 2.5 mg/ml Azocasein Azo-peptides , Peptides β€” β€” Classical aqueous control (in %)
Activity - Classical Activity measured by absorbance spectrophotometry (colorimetric assay, azo-peptide absorbance measurement, 340 nm) in the presence of organic solvent Acetone 30 % v/v 100 23 % Digital Continuous 100 mM citrate -Na2HPO4 buffer 5 40Β°C 2.5 mg/ml Azocasein Azo-peptides , Peptides β€” β€” Classical aqueous control (in %)
Activity - Classical Activity measured by absorbance spectrophotometry (colorimetric assay, azo-peptide absorbance measurement, 340 nm) in the presence of organic solvent Dimethyl Sulfoxide (DMSO) 15 % v/v 100 13 % Digital Continuous 100 mM citrate -Na2HPO4 buffer 5 40Β°C 2.5 mg/ml Azocasein Azo-peptides , Peptides β€” β€” Classical aqueous control (in %)
Activity - Classical Activity measured by absorbance spectrophotometry (colorimetric assay, azo-peptide absorbance measurement, 340 nm) in the presence of organic solvent Dimethyl Sulfoxide (DMSO) 30 % v/v 100 10 % Digital Continuous 100 mM citrate -Na2HPO4 buffer 5 40Β°C 2.5 mg/ml Azocasein Azo-peptides , 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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