HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 1.14.13.179 - methylxanthine N3-demethylase
for references in articles please use BRENDA:EC1.14.13.179Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The expected taxonomic range for this enzyme is: Pseudomonas putida
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
1.14.13.179
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
methylxanthine N3-demethylase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-methylxanthine + O2 + NAD(P)H + H+ = xanthine + NAD(P)+ + H2O + formaldehyde
(2)
-
3-methylxanthine + O2 + NAD(P)H + H+ = xanthine + NAD(P)+ + H2O + formaldehyde
(2)
-
-
3-methylxanthine + O2 + NAD(P)H + H+ = xanthine + NAD(P)+ + H2O + formaldehyde
-
-
-
-
theobromine + O2 + NAD(P)H + H+ = 7-methylxanthine + NAD(P)+ + H2O + formaldehyde
(1)
-
theobromine + O2 + NAD(P)H + H+ = 7-methylxanthine + NAD(P)+ + H2O + formaldehyde
(1)
-
-
theobromine + O2 + NAD(P)H + H+ = 7-methylxanthine + NAD(P)+ + H2O + formaldehyde
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
theobromine:oxygen oxidoreductase (N3-demethylating)
A non-heme iron oxygenase. The enzyme from the bacterium Pseudomonas putida shares an NAD(P)H-FMN reductase subunit with EC 1.14.13.178, methylxanthine N1-demethylase, and has higher activity with NADH than with NADPH [1]. Also demethylates caffeine and theophylline with lower efficiency. Forms part of the degradation pathway of methylxanthines.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
caffeine + O2 + NADH + H+
paraxanthine + NAD+ + H2O + formaldehyde
-
-
-
-
?
3-methylxanthine + O2 + NAD(P)H + H+
xanthine + NAD(P)+ + H2O + formaldehyde
-
-
-
?
3-methylxanthine + O2 + NAD(P)H + H+
xanthine + 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
-
-
?
3-methylxanthine + O2 + NAD(P)H + H+
xanthine + NAD(P)+ + H2O + formaldehyde
-
-
-
?
3-methylxanthine + O2 + NAD(P)H + H+
xanthine + 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
-
-
?
3-methylxanthine + O2 + NADH + H+
xanthine + NAD+ + H2O + formaldehyde
-
-
-
-
?
3-methylxanthine + O2 + NADH + H+
xanthine + NAD+ + H2O + formaldehyde
-
-
-
-
?
theobromine + O2 + NAD(P)H + H+
7-methylxanthine + NAD(P)+ + H2O + formaldehyde
-
-
-
?
theobromine + 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
-
-
?
theobromine + O2 + NAD(P)H + H+
7-methylxanthine + NAD(P)+ + H2O + formaldehyde
-
-
-
?
theobromine + 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
-
-
?
theobromine + O2 + NADH + H+
7-methylxanthine + NAD+ + H2O + formaldehyde
-
theobromine i.e. 3,7-dimethylxanthine
-
-
?
theobromine + O2 + NADH + H+
7-methylxanthine + NAD+ + H2O + formaldehyde
-
theobromine i.e. 3,7-dimethylxanthine
-
-
?
theophylline + O2 + NADH + H+
1-methylxanthine + NAD+ + H2O + formaldehyde
-
-
-
-
?
theophylline + O2 + NADH + H+
1-methylxanthine + NAD+ + H2O + formaldehyde
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
3-methylxanthine + O2 + NAD(P)H + H+
xanthine + 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
-
-
?
3-methylxanthine + O2 + NAD(P)H + H+
xanthine + 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
-
-
?
theobromine + 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
-
-
?
theobromine + 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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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 only 22% of that with NADH
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 only 22% of that with NADH
NADH
-
electron transfer from NADH via a redox-center-dense Rieske reductase, NdmD
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.179)
html completed
Use of this online version of BRENDA is free but requires a license. See terms of use.
Information
