Cytochrome P450 CYP152A1 from Bacillus subtilis

Enzyme Description

Extremophile
No
EC Number

Sequence

Length: 417 amino acids
MNEQIPHDKSLDNSLTLLKEGYLFIKNRTERYNSDLFQARLLGKNFICMTGAEAAKVFYDTDRFQRQNALPKRVQKSLFGVNAIQGMDGSAHIHRKMLFLSLMTPPHQKRLAELMTEEWKAAVTRWEKADEVVLFEEAKEILCRVACYWAGVPLKETEVKERADDFIDMVDAFGAVGPRHWKGRRARPRAEEWIEVMIEDARAGLLKTTSGTALHEMAFHTQEDGSQLDSRMAAIELINVLRPIVAISYFLVFSALALHEHPKYKEWLRSGNSREREMFVQEVRRYYPFGPFLGALVKKDFVWNNCEFKKGTSVLLDLYGTNHDPRLWDHPDEFRPERFAEREENLFDMIPQGGGHAEKGHRCPGEGITIEVMKASLDFLVHQIEYDVPEQSLHYSLARMPSLPESGFVMSGIRRKS
Kersten S. Rabe et al. (2010) β€” Peroxidase activity of bacterial cytochrome P450 enzymes: Modulation by fatty acids and organic solvents
Biotechnology Journal  Β· doi:10.1002/biot.201000028 β†—  Β· Activity - Classical
4 measurements
Database ID
UniProt: O31440 β†—
Sequence Annotation
Inferred
Protein Source
Recombinant, host bacterium Escherichia coli M15 (pREP4)

Experimental Data (4 measurements)

4 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 (in nmol substrate per nmol enzyme per second) measured by fluorescence spectrophotometry (resorufin fluorescence measurement) in the presence of organic solvent Methanol 10% 0.0205 0.0226 nmol substrate per nmol enzyme per second 50 mM potassium phosphate buffer 7 25Β°C 1 Β΅M Amplex red, 1 mM Hβ‚‚Oβ‚‚ (Hydrogen Peroxide) H2O , Resorufin β€” β€” Classical aqueous control (in nmol substrate per nmol enzyme per second)) | Here peroxidase activity measured, hence the EC number choice
Activity - Classical Activity (in nmol substrate per nmol enzyme per second) measured by fluorescence spectrophotometry (resorufin fluorescence measurement) in the presence of organic solvent Ethanol 10% 0.0205 0.0174 nmol substrate per nmol enzyme per second 50 mM potassium phosphate buffer 7 25Β°C 1 Β΅M Amplex red, 1 mM Hβ‚‚Oβ‚‚ (Hydrogen Peroxide) H2O , Resorufin β€” β€” Classical aqueous control (in nmol substrate per nmol enzyme per second)) | Here peroxidase activity measured, hence the EC number choice
Activity - Classical Activity (in nmol substrate per nmol enzyme per second) measured by fluorescence spectrophotometry (resorufin fluorescence measurement) in the presence of organic solvent Isopropanol 10% 0.0205 0.0088 nmol substrate per nmol enzyme per second 50 mM potassium phosphate buffer 7 25Β°C 1 Β΅M Amplex red, 1 mM Hβ‚‚Oβ‚‚ (Hydrogen Peroxide) H2O , Resorufin β€” β€” Classical aqueous control (in nmol substrate per nmol enzyme per second)) | Here peroxidase activity measured, hence the EC number choice
Activity - Classical Activity (in nmol substrate per nmol enzyme per second) measured by fluorescence spectrophotometry (resorufin fluorescence measurement) in the presence of organic solvent Acetonitrile 10% 0.0205 0.0139 nmol substrate per nmol enzyme per second 50 mM potassium phosphate buffer 7 25Β°C 1 Β΅M Amplex red, 1 mM Hβ‚‚Oβ‚‚ (Hydrogen Peroxide) H2O , Resorufin β€” β€” Classical aqueous control (in nmol substrate per nmol enzyme per second)) | Here peroxidase activity measured, hence the EC number choice

Visualization : Activity β€” Classical

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

Structure

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