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Literature summary for 1.6.2.4 extracted from

  • Inui, H.; Maeda, A.; Ohkawa, H.
    Molecular characterization of specifically active recombinant fused enzymes consisting of CYP3A4, NADPH-cytochrome P450 oxidoreductase, and cytochrome b5 (2007), Biochemistry, 46, 10213-10221.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
to analyze the molecular interaction among CYP3A4, NADPH-cytochrome P450 oxidoreductase, and b5, several fused enzyme genes are constructed and expressed in Saccharomyces cerevisiae. The recombinant fused enzymes CYP3A4-truncated(t)-P450 reductase-t-b5 (3RB) and CYP3A4-t-b5-t-P450 reductase (3BR) in yeast microsomes shows a higher specific activity in 6beta-hydroxylation of testosterone than does the reconstitution premixes of CYP3A4, P450 reductase, and b5. The purified fused enzymes exhibit lower Km values and substantially increased Vmax values in 6beta-hydroxylation of testosterone and oxidation of nifedipine. The fused enzymes shows significantly higher activities in cytochrome c reduction than the reconstitution premixes. Although the affinity of 3RB toward cytochrome c is twice as high as that of 3BR, 3BR and 3RB show nearly the same affinity toward NADPH/NADH. In addition, the heme of the CYP3A4 moiety of 3RB is reduced preferentially and more rapidly than that of 3BR, whereas the heme of the b5 moiety of 3BR is selectively reduced compared with that of 3RB Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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Synonyms

Synonyms Comment Organism
NADPH-cytochrome P450 oxidoreductase
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Saccharomyces cerevisiae
P450 reductase
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Saccharomyces cerevisiae