Cytochrome P450 CYP119 from Sulfolobus acidocaldarius

Enzyme Description

Extremophile
Yes thermoacidophilic organism

Sequence

Length: 368 amino acids
MYDWFSEMRKKDPVYYDGNIWQVFSYRYTKEVLNNFSKFSSDLTGYHERLEDLRNGKIRFDIPTRYTMLTSDPPLHDELRSMSADIFSPQKLQTLETFIRETTRSLLDSIDPREDDIVKKLAVPLPIIVISKILGLPIEDKEKFKEWSDLVAFRLGKPGEIFELGKKYLELIGYVKDHLNSGTEVVSRVVNSNLSDIEKLGYIILLLIAGNETTTNLISNSVIDFTRFNLWQRIREENLYLKAIEEALRYSPPVMRTVRKTKERVKLGDQTIEEGEYVRVWIASANRDEEVFHDGEKFIPDRNPNPHLSFGSGIHLCLGAPLARLEARIAIEEFSKRFRHIEILDTEKVPNEVLNGYKRLVVRLKSNE
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: Q55080 β†—
Sequence Annotation
Inferred
Protein Source
Recombinant, host bacterium Escherichia coli BL21 (DE3)

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% 0.0005 0.0025 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% 0.0005 0.0021 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% 0.0005 0.0034 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% 0.0005 0.0022 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

Kersten S. Rabe et al. (2010)

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

Tugce Sakalli et al. (2021) β€” Functional characterization of a novel CYP119 variant to explore its biocatalytic potential
Biotechnology and Applied Biochemistry  Β· doi:10.1002/bab.2243 β†—  Β· Activity - Classical
18 measurements

Structure

Drag to rotate Β· Scroll to zoom Β· Right-click drag to pan Β· Powered by Mol*