This cytochrome-P-450 enzyme, from the soil-dwelling bacterium Streptomyces coelicolor A3(2), catalyses two sequential allylic oxidation reactions. The substrate epi-isozizaene, which is formed by the action of EC 4.2.3.37, epi-isozizaene synthase, is first oxidized to yield the epimeric intermediates (5R)-albaflavenol and (5S)-albaflavenol, which can be further oxidized to yield the sesquiterpenoid antibiotic albaflavenone.
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The enzyme appears in viruses and cellular organisms
This cytochrome-P-450 enzyme, from the soil-dwelling bacterium Streptomyces coelicolor A3(2), catalyses two sequential allylic oxidation reactions. The substrate epi-isozizaene, which is formed by the action of EC 4.2.3.37, epi-isozizaene synthase, is first oxidized to yield the epimeric intermediates (5R)-albaflavenol and (5S)-albaflavenol, which can be further oxidized to yield the sesquiterpenoid antibiotic albaflavenone.
enzyme catalyses two sequential allylic oxidation reactions. The substrate epi-isozizaene is first oxidized to yield the epimeric intermediates (5R)-albaflavenol and (5S)-albaflavenol, which can be further oxidized to yield the sesquiterpenoid antibiotic albaflavenone. Proposed mechanism of biosynthesis of albaflavenone catalyzed by CYP170A1
the bifunctional enzyme is able to also generate farnesene isomers from farnesyl diphosphate: (E)-beta-farnesene (61%), (3E,6E)-alpha-farnesene (26%), (3Z,6E)-alpha-farnesene (6.8%), nerolidol (4.9%), and farnesol(1.8%)
enzyme catalyses two sequential allylic oxidation reactions. The substrate epi-isozizaene is first oxidized to yield the epimeric intermediates (5R)-albaflavenol and (5S)-albaflavenol, which can be further oxidized to yield the sesquiterpenoid antibiotic albaflavenone. Proposed mechanism of biosynthesis of albaflavenone catalyzed by CYP170A1
the bifunctional enzyme is able to also generate farnesene isomers from farnesyl diphosphate: (E)-beta-farnesene (61%), (3E,6E)-alpha-farnesene (26%), (3Z,6E)-alpha-farnesene (6.8%), nerolidol (4.9%), and farnesol(1.8%)
the bifunctional enzyme is able to also generate farnesene isomers from farnesyl diphosphate: (E)-beta-farnesene (61%), (3E,6E)-alpha-farnesene (26%), (3Z,6E)-alpha-farnesene (6.8%), nerolidol (4.9%), and farnesol(1.8%)
the bifunctional enzyme is able to also generate farnesene isomers from farnesyl diphosphate: (E)-beta-farnesene (61%), (3E,6E)-alpha-farnesene (26%), (3Z,6E)-alpha-farnesene (6.8%), nerolidol (4.9%), and farnesol(1.8%)