Disease relevance of CYP2W1

• The level of expression of human cytochrome P450 2W1 achieved using codon optimization for E. coli was 1800 nmol of cytochrome P450 per liter of culture, the highest level achieved in this laboratory to date [1].

High impact information on CYP2W1

• Cytochrome P450 2W1 catalyzed benzphetamine N-demethylation (k(cat), 3.8/min) and arachidonic acid oxidation, albeit at a very low rate (approximately 0.05/min) [1].
• Transfection of HEK293 cells with CYP2W1 caused the formation of a properly folded enzyme, which was catalytically active with arachidonic acid as a substrate [2].
• Re-expression of CYP2W1 was seen following demethylation by 5-Aza-2'-deoxycytidine [2].
• Recently, it was reported that CYP2W1 can metabolize arachidonic acid [3].
• Further analysis using an E. coli expression system will reveal substrate specificity of CYP2W1 and why this P450 isoform is universally conserved in vertebrates [3].

Biological context of CYP2W1

• The human genome project revealed a new member of the P450 family 2, CYP2W1, which has orthologous form in other vertebrate species, suggesting CYP2W1's significant physiological function [3].

Associations of CYP2W1 with chemical compounds

• Based on this result, we revealed that CYP2W1 catalyzes the oxidation of indole [3].
• In addition, CYP2W1 showed monooxygenase activity towards 3-methylindole and chlorzoxazone [3].

Other interactions of CYP2W1

• In the bicistronic expression system for human CYP2W1 and NADPH-P450 reductase, the formation of blue pigment, indigo, was observed in bacterial cultures [3].

Analytical, diagnostic and therapeutic context of CYP2W1

• Western blotting also revealed high expression of CYP2W1 in some human colon tumors [2].

References