The enzyme, characterized from the bacterium Streptomyces rimosus, is bifunctional, catalysing two successive monooxygenation reactions. It starts by catalysing the stereospecific hydroxylation of anhydrotetracycline at C-6 (EC 1.14.13.38). If the released product is captured by EC 1.3.98.4, 5a,11a-dehydrotetracycline dehydrogenase (OxyR), it is reduced to tetracycline. However, if the released product is recaptured by OxyS, it performs an additional hydroxylation at C-5, producing 5a,11a-dehydrooxytetracycline, which, following the action of OxyR, becomes oxytetracycline.
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The enzyme appears in viruses and cellular organisms
The enzyme, characterized from the bacterium Streptomyces rimosus, is bifunctional, catalysing two successive monooxygenation reactions. It starts by catalysing the stereospecific hydroxylation of anhydrotetracycline at C-6 (EC 1.14.13.38). If the released product is captured by EC 1.3.98.4, 5a,11a-dehydrotetracycline dehydrogenase (OxyR), it is reduced to tetracycline. However, if the released product is recaptured by OxyS, it performs an additional hydroxylation at C-5, producing 5a,11a-dehydrooxytetracycline, which, following the action of OxyR, becomes oxytetracycline.
bifunctional enzyme, catalyzes the stereospecific hydroxylation of anhydrotetracycline at C-6 (EC 1.14.13.38) and performs an additional hydroxylation at C-5, producing 5a,11a-dehydrooxytetracycline, reaction of EC 1.14.13.234
bifunctional enzyme, catalyzes the stereospecific hydroxylation of anhydrotetracycline at C-6 (EC 1.14.13.38) and performs an additional hydroxylation at C-5, producing 5a,11a-dehydrooxytetracycline, reaction of EC 1.14.13.234
bifunctional enzyme, catalyzes the stereospecific hydroxylation of anhydrotetracycline at C-6 (EC 1.14.13.38) and performs an additional hydroxylation at C-5, producing 5a,11a-dehydrooxytetracycline, reaction of EC 1.14.13.234
OxyS catalyzes two sequential hydroxylations at C6 and C5 positions of anhydrotetracycline with opposite stereochemistry. OxyS and reductase OxyR are sufficient to produce the mature tetracycline scaffold, i.e. the complete conversion of anhydrotetracycline to oxytetracycline and tetracycline. OxyS catalyzes the stereospecific hydroxylation of anhydrotetracycline at C-6 (reaction of EC 1.14.13.38). If the released product is captured by EC 1.3.98.4, 5a,11a-dehydrotetracycline dehydrogenase (OxyR), it is reduced to tetracycline. However, if the released product is recaptured by OxyS, it performs an additional hydroxylation at C-5, producing 5a,11a-dehydrooxytetracycline, which, following the action of OxyR, becomes oxytetracycline
when grown in media containing antimetabolites of compounds involved in biological ethylation reactions, Streptomyces aureofaciens produces a group of N-demethylanhydrotetracyclones. Sulfadiazine, L- and D-ethionine and a variety of methionine and homocysteine analogs cause the accumulation of precursors
when grown in media containing antimetabolites of compounds involved in biological ethylation reactions, Streptomyces aureofaciens produces a group of N-demethylanhydrotetracyclones. Sulfadiazine, L- and D-ethionine and a variety of methionine and homocysteine analogs cause the accumulation of precursors
when grown in media containing antimetabolites of compounds involved in biological ethylation reactions, Streptomyces aureofaciens produces a group of N-demethylanhydrotetracyclones. Sulfadiazine, L- and D-ethionine and a variety of methionine and homocysteine analogs cause the accumulation of precursors
OxyS catalyzes two sequential hydroxylations at C6 and C5 positions of anhydrotetracycline with opposite stereochemistry. OxyS and reductase OxyR are sufficient to produce the mature tetracycline scaffold, i.e. the complete conversion of anhydrotetracycline to oxytetracycline and tetracycline. OxyS catalyzes the stereospecific hydroxylation of anhydrotetracycline at C-6 (reaction of EC 1.14.13.38). If the released product is captured by EC 1.3.98.4, 5a,11a-dehydrotetracycline dehydrogenase (OxyR), it is reduced to tetracycline. However, if the released product is recaptured by OxyS, it performs an additional hydroxylation at C-5, producing 5a,11a-dehydrooxytetracycline, which, following the action of OxyR, becomes oxytetracycline
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of OxyS in complex with oxidized flavin to 2.6 A resolution. The monomeric OxyS is comprised of three structural domains, including the FAD-binding domain (residues 1-175 and 271-389), the middle domain (residues 176-270), and the C-terminal thioredoxin-like domain (residues 390?503). The tetracycline substrate is anchored in a narrow hydrophobic cleft at the interface between the FAD-binding and the middle domains
biosynthesis of tetracycline from anhydrotetracycline in Saccharomyces cerevisiae heterologously expressing the anhydrotetracycline hydroxylase OxyS, the dehydrotetracycline reductase CtcM, and the F420 reductase FNO from three bacterial hosts. This biosynthesis of tetracycline is enabled by OxyS performing just one hydroxylation step in S. cerevisiae
biosynthesis of tetracycline from anhydrotetracycline in Saccharomyces cerevisiae heterologously expressing the anhydrotetracycline hydroxylase OxyS, the dehydrotetracycline reductase CtcM, and the F420 reductase FNO from three bacterial hosts. This biosynthesis of tetracycline is enabled by OxyS performing just one hydroxylation step in S. cerevisiae
Enzyme Nomenclature
1.14.13.234 5a,11a-dehydrotetracycline 5-monooxygenase
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