The enzyme from the bacterium Streptomyces lincolnensis participates in the biosynthesis of the antibiotic lincomycin A, while that from Streptomyces refuineus is involved in anthramycin biosynthesis. The enzyme, which contains a heme b cofactor, is rapidly inactivated in the presence of hydrogen peroxide, but the presence of L-tyrosine protects it. cf. EC 1.11.2.5, 3-methyl-L-tyrosine peroxygenase.
The enzyme from the bacterium Streptomyces lincolnensis participates in the biosynthesis of the antibiotic lincomycin A, while that from Streptomyces refuineus is involved in anthramycin biosynthesis. The enzyme, which contains a heme b cofactor, is rapidly inactivated in the presence of hydrogen peroxide, but the presence of L-tyrosine protects it. cf. EC 1.11.2.5, 3-methyl-L-tyrosine peroxygenase.
the enzyme performs oxidative C-H bond cleavage at C5 to generate 3-chloro-5-hydroxyl-L-tyrosine and oxygenation at C3 concomitant with a carbon-fluorine bond cleavage to yield L-dopa and chloride
the enzyme performs oxidative C-H bond cleavage at C5 to generate 3-fluoro-5-hydroxyl-L-tyrosine and oxygenation at C3 concomitant with a carbon-fluorine bond cleavage to yield L-dopa and fluoride
the enzyme performs oxidative C-H bond cleavage at C5 to generate 3-iodo-5-hydroxyl-L-tyrosine and oxygenation at C3 concomitant with a carbon-fluorine bond cleavage to yield L-dopa and iodide
The genes ImbB1 and ImbB2 of Streptomyces lincolnensis encode enzymes involved in the conversion of L-tyrosine to propylproline during the biosynthesis of the antibiotic lincomycin A
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1.11.2.6 L-tyrosine peroxygenase
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