The enzyme, characterized from the bacterium Streptomyces rimosus, participates in the biosynthesis of tetracycline antibiotics. That bacterium possesses two enzymes that can catalyse the reaction - OxyE is the main isozyme, while OxyL has a lower activity. OxyL is bifunctional, and its main function is EC 1.14.13.233, 4-hydroxy-6-methylpretetramide 12a-monooxygenase. Contains FAD.
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The enzyme appears in viruses and cellular organisms
The enzyme, characterized from the bacterium Streptomyces rimosus, participates in the biosynthesis of tetracycline antibiotics. That bacterium possesses two enzymes that can catalyse the reaction - OxyE is the main isozyme, while OxyL has a lower activity. OxyL is bifunctional, and its main function is EC 1.14.13.233, 4-hydroxy-6-methylpretetramide 12a-monooxygenase. Contains FAD.
a gene disruption mutant reveals the complete disappearance of oxytetracycline, with the concomitant appearance of a predominant glycoside metabolite derived from 4-hydroxy-6-methylpretetramid; OxyE plays a nonessential, but important role in oxytetracycline biosynthesis by serving as a efficient C-4 hydroxylase. A gene disruption mutant produces only about 50% of the oxytetracycline found in wild-type, and additionally synthesizes a glycoside derivative of 6-methylpretetramide
a gene disruption mutant reveals the complete disappearance of oxytetracycline, with the concomitant appearance of a predominant glycoside metabolite derived from 4-hydroxy-6-methylpretetramid; OxyE plays a nonessential, but important role in oxytetracycline biosynthesis by serving as a efficient C-4 hydroxylase. A gene disruption mutant produces only about 50% of the oxytetracycline found in wild-type, and additionally synthesizes a glycoside derivative of 6-methylpretetramide; OxyL is a NADPH-dependent dioxygenase that hydroxylates 6-methylpretetramide at both C12a and C4 positions
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1.14.13.232 6-methylpretetramide 4-monooxygenase
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