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Enzyme Nomenclature
Information on EC 1.14.13.38 - anhydrotetracycline 6-monooxygenase
for references in articles please use BRENDA:EC1.14.13.38
Word Map on EC 1.14.13.38
- 1.14.13.38
- aureofaciens
- chlortetracycline
- rimosus
-
polyketide
- thiocyanate
-
benzyl
-
high-production
-
low-production
- pharmacology
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.13.38
-
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RECOMMENDED NAME
GeneOntology No.
anhydrotetracycline 6-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
anhydrotetracycline + NADPH + H+ + O2 = 12-dehydrotetracycline + NADP+ + H2O
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
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redox reaction
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-
-
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reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
anhydrotetracycline,NADPH:oxygen oxidoreductase (6-hydroxylating)
The enzyme, characterized from the bacterium Streptomyces rimosus, participates in the biosynthesis of tetracycline antibiotics. It can also catalyse EC 1.14.13.234, 12-dehydrotetracycline 5-monooxygenase.
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CAS REGISTRY NUMBER
COMMENTARY
70766-62-0
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
50/137, UV-light induced mutant of strain 84/25
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-
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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
anhydrotetracycline + NADPH + O2
12-dehydrotetracycline + NADP+ + H2O
-
-
-
-
?
anhydrotetracycline + NADPH + O2
12-dehydrotetracycline + NADP+ + H2O
-
-
-
?
anhydrotetracycline + NADPH + O2
12-dehydrotetracycline + NADP+ + H2O
-
-
-
?
anhydrotetracycline + NADPH + O2
12-dehydrotetracycline + NADP+ + H2O
-
-
-
?
anhydrotetracycline + NADPH + O2
12-dehydrotetracycline + NADP+ + H2O
-
tetracycline and chlortetracycline biosynthetic pathways
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-
?
anhydrotetracycline + NADPH + O2
12-dehydrotetracycline + NADP+ + H2O
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chlortetracycline biosynthetic pathway
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-
?
anhydrotetracycline + NADPH + O2
12-dehydrotetracycline + NADP+ + H2O
-
involved in the biosynthesis of tetracyclines
-
-
?
anhydrotetracycline + NADPH + O2
12-dehydrotetracycline + NADP+ + H2O
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-
-
?
anhydrotetracycline + NADPH + O2
12-dehydrotetracycline + NADP+ + H2O
the enzyme catalyzes a hydroxylation of the anthracycline structure at position C-6 after biosynthesis of the polyketide backbone is completed, Biosynthesis of oxytetracycline, overview
product identification
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
anhydrotetracycline + NADPH + O2
12-dehydrotetracycline + NADP+ + H2O
-
tetracycline and chlortetracycline biosynthetic pathways
-
-
?
anhydrotetracycline + NADPH + O2
12-dehydrotetracycline + NADP+ + H2O
-
chlortetracycline biosynthetic pathway
-
-
?
anhydrotetracycline + NADPH + O2
12-dehydrotetracycline + NADP+ + H2O
-
involved in the biosynthesis of tetracyclines
-
-
?
anhydrotetracycline + NADPH + O2
12-dehydrotetracycline + NADP+ + H2O
Q58PK7
the enzyme catalyzes a hydroxylation of the anthracycline structure at position C-6 after biosynthesis of the polyketide backbone is completed, Biosynthesis of oxytetracycline, overview
product identification
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
three essential glycine codons are located within the putative NADPH-binding domain
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiobis-(2-nitrobenzoic acid)
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40% inhibition at 1 mM, irreversible
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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addition of supernatant of Streptomyces aureofaciens or Streptomyces rimosus crude extract after boiling and centrifugation increases activity 7fold
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0000112
recombinant wild-type enzyme in Escherichia coli cell extract
additional information
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overview: different activities in various subcellular fractions
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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predominantly, high-production strain, distribution in the cell is influenced by benzylthiocyanate
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predominantly, high-production strain, distribution in the cell is influenced by benzylthiocyanate
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene otcC, DNA and amino acid sequence determination and analysis, expression of the glycine mutant enzyme in Escherichia coli strain BL21(DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
a otcC disruption mutant strain of Streptomyces rimosus synthesizes a novel C-17 polyketide, the ability to make a 19-carbon backbone in the mutant strain is restored when the inactive mutant enzyme, with three essential glycine residues of the NADH-binding domain mutated by site-directed mutagenesis, is expressed in the disruption mutant strain, thus the quarternary structure of the enzyme is required, not only the its activity, in the synthase complex
additional information
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a otcC disruption mutant strain of Streptomyces rimosus synthesizes a novel C-17 polyketide, the ability to make a 19-carbon backbone in the mutant strain is restored when the inactive mutant enzyme, with three essential glycine residues of the NADH-binding domain mutated by site-directed mutagenesis, is expressed in the disruption mutant strain, thus the quarternary structure of the enzyme is required, not only the its activity, in the synthase complex
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.38)
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