Information on EC 1.14.13.234 - 5a,11a-dehydrotetracycline 5-monooxygenase

for references in articles please use BRENDA:EC1.14.13.234
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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.13.234
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RECOMMENDED NAME
GeneOntology No.
5a,11a-dehydrotetracycline 5-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5a,11a-dehydrotetracycline + NADPH + H+ + O2 = 5a,11a-dehydrooxytetracycline + NADP+ + H2O
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
tetracycline and oxytetracycline biosynthesis
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Tetracycline biosynthesis
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Biosynthesis of type II polyketide products
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
5a,11a-dehydrotetracycline,NADPH:oxygen oxidoreductase (5-hydroxylating)
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
UniProt
Manually annotated by BRENDA team
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
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5a,11a-dehydrotetracycline + NADPH + H+ + O2
5a,11a-dehydrooxytetracycline + NADP+ + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57500
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2 * 57500, SDS-PAGE
115000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 57500, SDS-PAGE
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
60fold purification in a 40% yield, using a combination of hydrophobic chromatography and ion-exchange HPLC
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Streptomyces lividans and Escherichia coli