{'fraction_non_alphanumeric': 0.03518518518518519, 'fraction_numerical': 0.046296296296296294, 'mean_word_length': 5.364705882352941, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Cloning, Expression in Yeast, and Functional Characterization of CYP76A4, a Novel Cytochrome P450 of Petunia That Catalyzes (ω-1)-Hydroxylation of Lauric Acid

A cDNA clone of a novel cytochrome P450, CYP76A4, was isolated from Petunia hybrida. The cDNA clone contained an open reading frame (ORF) encoding a predicted 510 amino acid polypeptide. The CYP76A4 cDNA was expressed in yeast Saccharomyces cerevisiae AH22. Recombinant yeast microsomes containing the CYP76A4 hemoprotein were found to catalyze (ω-1)-hydroxylation of lauric acid.