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Information on EC 1.14.13.38 - anhydrotetracycline 6-monooxygenase
for references in articles please use BRENDA:EC1.14.13.38
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
1.14.13.38 anhydrotetracycline 6-monooxygenase
IUBMB 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.
The enzyme appears in viruses and cellular organisms
- 1.14.13.38
- aureofaciens
- chlortetracycline
- low-production
- thiocyanate
-
benzyl
- rimosus
- polyketide
-
high-production
- pharmacology
showSynonyms
anhydrotetracycline oxygenase, anhydrotetracycline hydroxylase, anhydrotetracycline monooxygenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
anhydrotetracycline monooxygenase
-
-
ambiguous
-
anhydrotetracycline oxygenase
ATC oxygenase
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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
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
tetracycline and oxytetracycline biosynthesis
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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
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
anhydrooxytetracycline + NADPH + O2
?
-
Substrates: -
Products: -
Products: -
?
anhydrotetracycline + NADPH + H+ + O2
12-dehydrotetracycline + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
anhydrotetracycline + NADPH + H+ + O2
5a,11a-dehydrotetracycline + NADP+ + H2O
Substrates: -
Products: -
Products: -
?
anhydrotetracycline + NADPH + H+ + O2
5a,11a-dehydrotetracycline + NADP+ + H2O
Substrates: -
Products: -
Products: -
?
anhydrotetracycline + NADPH + O2
12-dehydrotetracycline + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
anhydrotetracycline + NADPH + O2
12-dehydrotetracycline + NADP+ + H2O
-
Substrates: tetracycline and chlortetracycline biosynthetic pathways
Products: -
Products: -
?
anhydrotetracycline + NADPH + O2
12-dehydrotetracycline + NADP+ + H2O
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Substrates: chlortetracycline biosynthetic pathway
Products: -
Products: -
?
anhydrotetracycline + NADPH + O2
12-dehydrotetracycline + NADP+ + H2O
-
Substrates: involved in the biosynthesis of tetracyclines
Products: -
Products: -
?
anhydrotetracycline + NADPH + O2
12-dehydrotetracycline + NADP+ + H2O
Substrates: -
Products: -
Products: -
?
anhydrotetracycline + NADPH + O2
12-dehydrotetracycline + NADP+ + H2O
Substrates: 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
Products: product identification
Products: product identification
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
anhydrotetracycline + NADPH + H+ + O2
12-dehydrotetracycline + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
anhydrotetracycline + NADPH + O2
12-dehydrotetracycline + NADP+ + H2O
-
Substrates: tetracycline and chlortetracycline biosynthetic pathways
Products: -
Products: -
?
anhydrotetracycline + NADPH + O2
12-dehydrotetracycline + NADP+ + H2O
-
Substrates: chlortetracycline biosynthetic pathway
Products: -
Products: -
?
anhydrotetracycline + NADPH + O2
12-dehydrotetracycline + NADP+ + H2O
-
Substrates: involved in the biosynthesis of tetracyclines
Products: -
Products: -
?
anhydrotetracycline + NADPH + O2
12-dehydrotetracycline + NADP+ + H2O
Substrates: 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
Products: product identification
Products: 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
-
predominantly, high-production strain, distribution in the cell is influenced by benzylthiocyanate
brenda
-
predominantly, high-production strain, distribution in the cell is influenced by benzylthiocyanate
-
brenda
-
predominantly, low-production strain
-
brenda
Highest Expressing Human Cell Lines
Cell Line Links Show AA Sequence and Transmembrane Helices (127 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
additional information
-
recombinant overexpression of gene oxySin Saccharomyces cerevisiae, functional coexpression with heterologous dehydrotetracycline reductase CtcM, and the F420 reductase FNO. Biosynthesis of tetracycline is enabled by OxyS performing just one hydroxylation step in Saccharomyces cerevisiae despite its previous characterization as a double hydroxylase. This single hydroxylation enables the purification and structural characterization of a hypothetical intermediate in oxytetracycline biosynthesis that can explain structural differences between oxytetracycline and chlortetracycline. Using the alternative enzyme CtcM from the chlortetracycline pathway instead of OxyR yields in vitro an increased ratio of tetracycline to oxytetracycline. A unique cofactor to the last steps of the tetracyclines' biosynthesis that is not native to Saccharomyces cerevisiae is cofactor F420, a lactyl oligoglutamate phosphodiester derivative of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (Fo). Fo is much more synthetically accessible than F420. Fo can replace F420 in tetracycline biosynthesis. Three F420 reductase candidates from Mycobacterium tuberculosis, Archaeoglobus fulgidus, and Streptomyces griseus are explored, and the enzyme from Archaeoglobus fulgidus is chosen. Method development and evaluation, method optimization, overview
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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)
gene oxyS, functional recombinant overexpression of C-terminally FLAG-tagged enzyme in Saccharomyces cerevisiae from plasmid pSP-G1 resulting in biosynthesis of dehydrotetracycline from anhydrotetracycline, functional coexpression with heterologous dehydrotetracycline reductase CtcM, and the F420 reductase FNO
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
biosynthesis of tetracycline from anhydrotetracycline in Saccharomyces cerevisiae heterologously expressing the anhydrotetracycline hydroxylase OxyS, the dehydrotetracycline reductase CtcM, and the F420 reductase FNO from three bacterial hosts. This biosynthesis of tetracycline is enabled by OxyS performing just one hydroxylation step in S. cerevisiae
synthesis
-
biosynthesis of tetracycline from anhydrotetracycline in Saccharomyces cerevisiae heterologously expressing the anhydrotetracycline hydroxylase OxyS, the dehydrotetracycline reductase CtcM, and the F420 reductase FNO from three bacterial hosts. This biosynthesis of tetracycline is enabled by OxyS performing just one hydroxylation step in S. cerevisiae
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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
Herbst, E.; Lee, A.; Tang, Y.; Snyder, S.; Cornish, V.
Heterologous catalysis of the final steps of tetracycline biosynthesis by Saccharomyces cerevisiae
ACS Chem. Biol.
16
1425-1434
2021
Streptomyces sp., Streptomyces rimosus subsp. rimosus (L8EUQ6), Streptomyces rimosus subsp. rimosus DSM 40260 (L8EUQ6)
brenda
EXTERNAL LINKS (specific for EC-Number 1.14.13.38)
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