Cysteine protease from Ervatamia coronaria
Enzyme Description
Sequence
LPEQIDWRKKGAVTPVKNQGSCGSCWAFSTVSTVESINQIRTGNLISLSEQELVDCDKKNHGCLGGAFVFAYQYIINNGGIDTQANYPYKAVQGPCQAASKVVSIDGYNGVPFCNEXALKQAVAVQPSTVAIDASSAQFQQYSSGIFSGPCGTKLNHGVTIVGYQANYWIVRNSWGRYWGEKGYIRMLRVGGCGLCGIARLPYYPTKA
Monica Sundd et al. (1998)
β Purification and Characterization of a Highly Stable Cysteine Protease from the Latex of Ervatamia coronaria
Bioscience, Biotechnology, and Biochemistry
Β· doi:10.1271/bbb.62.1947 β
Β· Activity - Classical
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Database ID
UniProt: P83654 β
Sequence Annotation
Inferred - from protein name
Protein Source
Purified, eukaryote Ervatamia coronaria
Experimental Data (3 measurements)
3 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, azopeptides absorbance measurement, 440 nm) in the presence of organic solvent | Acetonitrile | 40% | 100 | 100 | % | 0.05 M Tris-HCl | 8 | 37Β°C | ? mM Azoalbumin | azopeptides , Peptides | β | β | Classical aqueous control (in %) |
| Activity - Classical | Activity measured by absorbance spectrophotometry (colorimetric assay, azopeptides absorbance measurement, 440 nm) in the presence of organic solvent | Ethanol | 70% | 100 | 100 | % | 0.05 M Tris-HCl | 8 | 37Β°C | ? mM Azoalbumin | azopeptides , Peptides | β | β | Classical aqueous control (in %) |
| Activity - Classical | Activity measured by absorbance spectrophotometry (colorimetric assay, azopeptides absorbance measurement, 440 nm) in the presence of organic solvent | Methanol | 50% | 100 | 100 | % | 0.05 M Tris-HCl | 8 | 37Β°C | ? mM Azoalbumin | azopeptides , Peptides | β | β | Classical aqueous control (in %) |
Visualization : Activity β Classical
One bar per measurement. Colour = solvent, shade = solvent volume.