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Information on EC 1.14.13.38 - anhydrotetracycline 6-monooxygenase
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1.14.13.38 anhydrotetracycline 6-monooxygenaseIUBMB Comments
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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Word Map
- 1.14.13.38
- aureofaciens
- chlortetracycline
- rimosus
-
high-production
-
benzyl
- thiocyanate
- polyketide
- low-production
- pharmacology
The enzyme appears in viruses and cellular organisms
Synonyms
anhydrotetracycline monooxygenase, anhydrotetracycline oxygenase, ATC oxygenase, oxygenase, anhydrotetracycline, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
anhydrotetracycline monooxygenase
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ambiguous
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anhydrotetracycline oxygenase
ATC oxygenase
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-
-
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oxygenase, anhydrotetracycline
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-
-
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anhydrotetracycline oxygenase
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-
-
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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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redox reaction
-
-
-
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reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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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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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
-
-
?
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
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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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?
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NATURAL SUBSTRATE
NATURAL 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
-
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
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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiobis-(2-nitrobenzoic acid)
-
40% inhibition at 1 mM, irreversible
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
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
-
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
50/137, UV-light induced mutant of strain 84/25
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-
brenda
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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
brenda
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predominantly, high-production strain, distribution in the cell is influenced by benzylthiocyanate
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brenda
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predominantly, low-production strain
-
brenda
Show AA Sequence and Transmembrane Helices (132 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
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
-
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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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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vancurova, I.; Flieger, M.; Volc, J.; Benes, M.J.; Novotna, J.; Neuzil, J.; Behal, V.
Partial purification and characterization of anhydrotetracycline oxygenase of Streptomyces aureofaciens
J. Basic Microbiol.
27
529-533
1987
Kitasatospora aureofaciens
brenda
Behal, V.; Neuzil, J.; Hostalek, Z.
Effect of tetracycline derivates and some cations on the activity of anhydrotetracycline oxygenase
Biotechnol. Lett.
5
537-542
1983
Kitasatospora aureofaciens
-
brenda
Vancurova, I.; Volc, J.; Flieger, M.; Neuzil, J.; Novotna, J.; Vlach, J.; Behal, V.
Isolation of pure anhydrotetracycline oxygenase from Streptomyces aureofaciens
Biochem. J.
253
263-267
1988
Kitasatospora aureofaciens
brenda
Neuzil, J.; Novotna, J.; Vancurova, I.; Behal, V.; Hostalek, Z.
A direct-injection reversed-phase liquid chromatographic micromethod for studying the kinetics of terminal reactions of tetracycline biosynthesis
Anal. Biochem.
181
125-129
1989
Kitasatospora aureofaciens
brenda
Erban, V.; Trilisenko, L.V.; Novotna, J.; Behal, V.; Kulaev, I.S.; Hostalek, Z.
Subcellular localization if enzymes in Streptomyces areofaciens and its alteration by benzyl thiocyanate
Folia Microbiol. (Praha)
32
411-416
1987
Kitasatospora aureofaciens, Kitasatospora aureofaciens low-production
brenda
Behal, V.; Gregrova-Prusakova, J.; Hostalek, Z.
Effect of inorganic phosphate and benzyl thiocyanate of the activity of anhydrotetracycline oxygenase in Streptomyces aureofaciens
Folia Microbiol. (Praha)
27
102-106
1982
Kitasatospora aureofaciens
brenda
Li, X.M.; Novotna, J.; Vohradsky, J.; Weiser, J.
Major proteins related to chlortetracycline biosynthesis in a Streptomyces aureofaciens production strain studied by quantitative proteomics
Appl. Microbiol. Biotechnol.
57
717-724
2001
Kitasatospora aureofaciens
brenda
Peric-Concha, N.; Borovicka, B.; Long, P.F.; Hranueli, D.; Waterman, P.G.; Hunter, I.S.
Ablation of the otcC gene encoding a post-polyketide hydroxylase from the oxytetracyline biosynthetic pathway in Streptomyces rimosus results in novel polyketides with altered chain length
J. Biol. Chem.
280
37455-37460
2005
Streptomyces rimosus (Q58PK7), Streptomyces rimosus
brenda
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