Functional Characterization of Drosophila melanogaster CYP6A8 Fatty Acid Hydroxylase.

ABSTRACT: Genomic analysis indicated that the genome of Drosophila melanogaster contains more than 80 cytochrome P450 genes. To date, the enzymatic activity of these P450s has not been extensively studied. Here, the biochemical properties of CYP6A8 were characterized. CYP6A8 was cloned into the pCW vector, and its recombinant enzyme was expressed in Escherichia coli and purified using Ni²⁺-nitrilotriacetate affinity chromatography. Its expression level was approximately 130 nmol per liter of culture. Purified CYP6A8 exhibited a low-spin state in the absolute spectra of the ferric forms. Binding titration analysis indicated that lauric acid and capric acid produced type І spectral changes, with K_d values 28 ± 4 and 144 ± 20 μM, respectively. Ultra-per

SUBMITTER: Lee SA 

PROVIDER: S-EPMC9810445 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature