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Enzyme Nomenclature
Information on EC 1.14.13.178 - methylxanthine N1-demethylase
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.14.13.178
-
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RECOMMENDED NAME
GeneOntology No.
methylxanthine N1-demethylase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
caffeine + O2 + NAD(P)H + H+ = theobromine + NAD(P)+ + H2O + formaldehyde
(1)
-
caffeine + O2 + NAD(P)H + H+ = theobromine + NAD(P)+ + H2O + formaldehyde
(1)
-
-
caffeine + O2 + NAD(P)H + H+ = theobromine + NAD(P)+ + H2O + formaldehyde
-
-
-
-
paraxanthine + O2 + NAD(P)H + H+ = 7-methylxanthine + NAD(P)+ + H2O + formaldehyde
(3)
-
paraxanthine + O2 + NAD(P)H + H+ = 7-methylxanthine + NAD(P)+ + H2O + formaldehyde
(3)
-
-
paraxanthine + O2 + NAD(P)H + H+ = 7-methylxanthine + NAD(P)+ + H2O + formaldehyde
-
-
-
-
theophylline + O2 + NAD(P)H + H+ = 3-methylxanthine + NAD(P)+ + H2O + formaldehyde
(2)
-
theophylline + O2 + NAD(P)H + H+ = 3-methylxanthine + NAD(P)+ + H2O + formaldehyde
(2)
-
-
theophylline + O2 + NAD(P)H + H+ = 3-methylxanthine + NAD(P)+ + H2O + formaldehyde
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
caffeine:oxygen oxidoreductase (N1-demethylating)
A non-heme iron oxygenase. The enzyme from the bacterium Pseudomonas putida shares an NAD(P)H-FMN reductase subunit with EC 1.14.13.179, methylxanthine N3-demethylase, and has a 5-fold higher activity with NADH than with NADPH [2]. Also demethylate 1-methylxantine with lower efficiency. Forms part of the degradation pathway of methylxanthines.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
the enzyme forms part of the degradation pathway of methylxanthines
physiological function
-
the enzyme forms part of the degradation pathway of methylxanthines
-
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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
1-methylxanthine + O2 + NADH + H+
xanthine + NAD+ + H2O + formaldehyde
-
-
-
-
?
paraxanthine + O2 + NADH + H+
7-methylxanthine + NAD+ + H2O + formaldehyde
-
-
-
-
?
theophylline + O2 + NADPH + H+
3-methylxanthine + NADP+ + H2O + formaldehyde
-
i.e. 1,3-dimethylxanthine
-
-
?
caffeine + O2 + NAD(P)H + H+
theobromine + NAD(P)+ + H2O + formaldehyde
-
-
-
?
caffeine + O2 + NAD(P)H + H+
theobromine + NAD(P)+ + H2O + formaldehyde
-
the enzyme forms part of the degradation pathway of methylxanthines. The activity of the enzyme is dependent on electron transfer from NADH via a redox-center-dense Rieske reductase, NdmD
-
-
?
caffeine + O2 + NAD(P)H + H+
theobromine + NAD(P)+ + H2O + formaldehyde
-
-
-
?
caffeine + O2 + NAD(P)H + H+
theobromine + NAD(P)+ + H2O + formaldehyde
-
the enzyme forms part of the degradation pathway of methylxanthines. The activity of the enzyme is dependent on electron transfer from NADH via a redox-center-dense Rieske reductase, NdmD
-
-
?
caffeine + O2 + NADH + H+
theobromine + NAD+ + H2O + formaldehyde
-
the activity of the enzyme is dependent on electron transfer from NADH via a redox-center-dense Rieske reductase, NdmD
-
-
?
caffeine + O2 + NADH + H+
theobromine + NAD+ + H2O + formaldehyde
-
the activity of the enzyme is dependent on electron transfer from NADH via a redox-center-dense Rieske reductase, NdmD
-
-
?
paraxanthine + O2 + NAD(P)H + H+
7-methylxanthine + NAD(P)+ + H2O + formaldehyde
-
-
-
?
paraxanthine + O2 + NAD(P)H + H+
7-methylxanthine + NAD(P)+ + H2O + formaldehyde
-
the enzyme forms part of the degradation pathway of methylxanthines. The activity of the enzyme is dependent on electron transfer from NADH via a redox-center-dense Rieske reductase, NdmD
-
-
?
paraxanthine + O2 + NAD(P)H + H+
7-methylxanthine + NAD(P)+ + H2O + formaldehyde
-
-
-
?
paraxanthine + O2 + NAD(P)H + H+
7-methylxanthine + NAD(P)+ + H2O + formaldehyde
-
the enzyme forms part of the degradation pathway of methylxanthines. The activity of the enzyme is dependent on electron transfer from NADH via a redox-center-dense Rieske reductase, NdmD
-
-
?
theophylline + O2 + NAD(P)H + H+
3-methylxanthine + NAD(P)+ + H2O + formaldehyde
-
-
-
?
theophylline + O2 + NAD(P)H + H+
3-methylxanthine + NAD(P)+ + H2O + formaldehyde
-
the enzyme forms part of the degradation pathway of methylxanthines. The activity of the enzyme is dependent on electron transfer from NADH via a redox-center-dense Rieske reductase, NdmD
-
-
?
theophylline + O2 + NAD(P)H + H+
3-methylxanthine + NAD(P)+ + H2O + formaldehyde
-
-
-
?
theophylline + O2 + NADH + H+
3-methylxanthine + NAD+ + H2O + formaldehyde
-
-
-
-
?
theophylline + O2 + NADH + H+
3-methylxanthine + NAD+ + H2O + formaldehyde
-
-
-
-
?
additional information
?
-
-
no activity with theobromine, 3-methylxanthine and 7-methylxanthine
-
-
-
additional information
?
-
-
no activity with theobromine, 3-methylxanthine and 7-methylxanthine
-
-
-
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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
theophylline + O2 + NAD(P)H + H+
3-methylxanthine + NAD(P)+ + H2O + formaldehyde
-
the enzyme forms part of the degradation pathway of methylxanthines. The activity of the enzyme is dependent on electron transfer from NADH via a redox-center-dense Rieske reductase, NdmD
-
-
?
theophylline + O2 + NADPH + H+
3-methylxanthine + NADP+ + H2O + formaldehyde
-
i.e. 1,3-dimethylxanthine
-
-
?
caffeine + O2 + NAD(P)H + H+
theobromine + NAD(P)+ + H2O + formaldehyde
-
the enzyme forms part of the degradation pathway of methylxanthines. The activity of the enzyme is dependent on electron transfer from NADH via a redox-center-dense Rieske reductase, NdmD
-
-
?
caffeine + O2 + NAD(P)H + H+
theobromine + NAD(P)+ + H2O + formaldehyde
-
the enzyme forms part of the degradation pathway of methylxanthines. The activity of the enzyme is dependent on electron transfer from NADH via a redox-center-dense Rieske reductase, NdmD
-
-
?
paraxanthine + O2 + NAD(P)H + H+
7-methylxanthine + NAD(P)+ + H2O + formaldehyde
-
the enzyme forms part of the degradation pathway of methylxanthines. The activity of the enzyme is dependent on electron transfer from NADH via a redox-center-dense Rieske reductase, NdmD
-
-
?
paraxanthine + O2 + NAD(P)H + H+
7-methylxanthine + NAD(P)+ + H2O + formaldehyde
-
the enzyme forms part of the degradation pathway of methylxanthines. The activity of the enzyme is dependent on electron transfer from NADH via a redox-center-dense Rieske reductase, NdmD
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
-
a reductase component with cytochrome c reductase activity transfers reducing equivalents from NAD(P)H to the enzyme. NADH is the preferred substrate of the reductase component. Activity with NADPH is 22% of that with NADH
NADH
-
electron transfer from NADH via a redox-center-dense Rieske reductase, NdmD
NADPH
-
a reductase component with cytochrome c reductase activity transfers reducing equivalents from NAD(P)H to the enzyme. NADH is the preferred substrate of the reductase component. Activity with NADPH is 22% of that with NADH
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Non-heme iron
Non-heme iron
-
a non-heme iron oxygenase. Contains approximately 2 mol of acid labile sulfur and 2 mol of iron per mol of enzyme monomer
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the soluble N-demethylase holoenzyme is composed of two components, a reductase component with cytochrome c reductase activity (Ccr) and a two-subunit N-demethylase component (Ndm). Ndm, with a native molecular mass of 240000 Da, is composed of NdmA (40000 Da) and NdmB (35000 Da). Ccr transfers reducing equivalents from NAD(P)H to Ndm, which catalyses an oxygen-dependent N-demethylation of methylxanthines to xanthine, formaldehyde and water
additional information
-
the soluble N-demethylase holoenzyme is composed of two components, a reductase component with cytochrome c reductase activity (Ccr) and a two-subunit N-demethylase component (Ndm). Ndm, with a native molecular mass of 240000 Da, is composed of NdmA (40000 Da) and NdmB (35000 Da). Ccr transfers reducing equivalents from NAD(P)H to Ndm, which catalyses an oxygen-dependent N-demethylation of methylxanthines to xanthine, formaldehyde and water
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.178)
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