Title : Biochemical characterization of lauric acid omega-hydroxylation by a CYP4A1/NADPH-cytochrome P450 reductase fusion protein.

Pub. Date : 1995 Feb 20

PMID : 7872779






3 Functional Relationships(s)
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Protein Name
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1 Biochemical characterization of lauric acid omega-hydroxylation by a CYP4A1/NADPH-cytochrome P450 reductase fusion protein. lauric acid cytochrome P450, family 4, subfamily a, polypeptide 1 Rattus norvegicus
2 The binding and hydroxylation of lauric acid by a genetically engineered and expressed fusion protein comprised of an N-truncated form of rat CYP4A1 linked to an N-truncated form of rat NADPH cytochrome P450 oxidoreductase (OR) (constructed by Fisher et al., (1992) Proc. lauric acid cytochrome P450, family 4, subfamily a, polypeptide 1 Rattus norvegicus
3 (omega-1)-Hydroxylation of lauric acid was barely detectable (omega/(omega-1) = 135) with f4A1 or with reconstituted CYP4A1, but it accounted for up to 50% of total products formed by microsomes from clofibrate-induced rats. lauric acid cytochrome P450, family 4, subfamily a, polypeptide 1 Rattus norvegicus