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Enzyme Nomenclature
Information on EC 1.14.13.232 - 6-methylpretetramide 4-monooxygenase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.13.232
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RECOMMENDED NAME
GeneOntology No.
6-methylpretetramide 4-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
6-methylpretetramide + NADPH + H+ + O2 = 4-hydroxy-6-methylpretetramide + NADP+ + H2O
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
6-methylpretetramide,NADPH:oxygen oxidoreductase (4-hydroxylating)
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
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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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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; 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
physiological function
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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; 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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
6-methylpretetramide + NADPH + H+ + O2
4-hydroxy-6-methylpretetramide + NADP+ + H2O
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?
6-methylpretetramide + NADPH + H+ + O2
4-hydroxy-6-methylpretetramide + NADP+ + H2O
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?
6-methylpretetramide + NADPH + H+ + O2
4-hydroxy-6-methylpretetramide + NADP+ + H2O
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?
6-methylpretetramide + NADPH + H+ + O2
4-hydroxy-6-methylpretetramide + NADP+ + H2O
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.232)
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