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EC Tree
IUBMB Comments Contains FAD. The enzyme, characterized from the bacterium Streptomyces rimosus, participates in the biosynthesis of tetracycline antibiotics. The enzyme is bifunctional, and can also catalyse EC 1.14.13.232, 6-methylpretetramide 4-monooxygenase.
The expected taxonomic range for this enzyme is: Streptomyces rimosus
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oxyL
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4-hydroxy-6-methylpretetramide + NADPH + H+ + O2 = 4-de(dimethylamino)-4-oxoanhydrotetracycline + NADP+ + H2O
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4-hydroxy-6-methylpretetramide,NADPH:oxygen oxidoreductase (12a-hydroxylating)
Contains FAD. The enzyme, characterized from the bacterium Streptomyces rimosus, participates in the biosynthesis of tetracycline antibiotics. The enzyme is bifunctional, and can also catalyse EC 1.14.13.232, 6-methylpretetramide 4-monooxygenase.
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4-hydroxy-6-methylpretetramide + NADPH + H+ + O2
4-de(dimethylamino)-4-oxoanhydrotetracycline + NADP+ + H2O
4-hydroxy-6-methylpretetramide + NADPH + H+ + O2
4-de(dimethylamino)-4-oxoanhydrotetracycline + NADP+ + H2O
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4-hydroxy-6-methylpretetramide + NADPH + H+ + O2
4-de(dimethylamino)-4-oxoanhydrotetracycline + NADP+ + H2O
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4-hydroxy-6-methylpretetramide + NADPH + H+ + O2
4-de(dimethylamino)-4-oxoanhydrotetracycline + NADP+ + H2O
4-hydroxy-6-methylpretetramide + NADPH + H+ + O2
4-de(dimethylamino)-4-oxoanhydrotetracycline + NADP+ + H2O
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4-hydroxy-6-methylpretetramide + NADPH + H+ + O2
4-de(dimethylamino)-4-oxoanhydrotetracycline + NADP+ + H2O
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bifunctional enzyme, hydroxylates 6-methylpretetramide at both the C-12a and C-4 positions, i.e. reactions of EC 1.14.13.232 and EC 1.14.1.3.233
UniProt
brenda
bifunctional enzyme, hydroxylates 6-methylpretetramide at both the C-12a and C-4 positions, i.e. reactions of EC 1.14.13.232 and EC 1.14.1.3.233
UniProt
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physiological function
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
physiological function
OxyL is a NADPH-dependent dioxygenase that hydroxylates 6-methylpretetramide at both C12a and C4 positions
physiological function
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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
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physiological function
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OxyL is a NADPH-dependent dioxygenase that hydroxylates 6-methylpretetramide at both C12a and C4 positions
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OXYL_STRRM
557
0
59624
Swiss-Prot
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expression in Escherichia coli
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Wang, P.; Zhang, W.; Zhan, J.; Tang, Y.
Identification of oxyE as an ancillary oxygenase during tetracycline biosynthesis
ChemBioChem
10
1544-1550
2009
Streptomyces rimosus (Q3S8Q4), Streptomyces rimosus ATCC 10970 (Q3S8Q4)
brenda
Zhang, W.; Watanabe, K.; Cai, X.; Jung, M.; Tang, Y.; Zhan, J.
Identifying the minimal enzymes required for anhydrotetracycline biosynthesis
J. Am. Chem. Soc.
130
6068-6069
2008
Streptomyces rimosus (Q3S8Q4), Streptomyces rimosus ATCC 10970 (Q3S8Q4)
brenda
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Enzyme Nomenclature
1.14.13.233 4-hydroxy-6-methylpretetramide 12a-monooxygenase
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