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Information on EC 1.14.13.178 - methylxanthine N1-demethylase and Organism(s) Pseudomonas putida and UniProt Accession H9N289

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IUBMB Comments
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 . Also demethylate 1-methylxantine with lower efficiency. Forms part of the degradation pathway of methylxanthines.
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This record set is specific for:
Pseudomonas putida
UNIPROT: H9N289
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The taxonomic range for the selected organisms is: Pseudomonas putida
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
methylxanthine n1-demethylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
caffeine + O2 + NAD(P)H + H+ = theobromine + NAD(P)+ + H2O + formaldehyde
show the reaction diagram
(1)
theophylline + O2 + NAD(P)H + H+ = 3-methylxanthine + NAD(P)+ + H2O + formaldehyde
show the reaction diagram
(2)
paraxanthine + O2 + NAD(P)H + H+ = 7-methylxanthine + NAD(P)+ + H2O + formaldehyde
show the reaction diagram
(3)
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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-methylxanthine + O2 + NADH + H+
xanthine + NAD+ + H2O + formaldehyde
show the reaction diagram
-
-
-
?
caffeine + O2 + NAD(P)H + H+
theobromine + NAD(P)+ + H2O + formaldehyde
show the reaction diagram
caffeine + O2 + NADH + H+
theobromine + NAD+ + H2O + formaldehyde
show the reaction diagram
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
show the reaction diagram
paraxanthine + O2 + NADH + H+
7-methylxanthine + NAD+ + H2O + formaldehyde
show the reaction diagram
-
-
-
?
theophylline + O2 + NAD(P)H + H+
3-methylxanthine + NAD(P)+ + H2O + formaldehyde
show the reaction diagram
theophylline + O2 + NADH + H+
3-methylxanthine + NAD+ + H2O + formaldehyde
show the reaction diagram
-
-
-
?
additional information
?
-
no activity with theobromine, 3-methylxanthine and 7-methylxanthine
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
caffeine + O2 + NAD(P)H + H+
theobromine + NAD(P)+ + H2O + formaldehyde
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
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 22% of that with NADH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
non-heme iron
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.27
1-Methylxanthine
pH 7.5, 30°C
0.037
Caffeine
pH 7.5, 30°C
0.053
paraxanthine
pH 7.5, 30°C
0.0091
theophylline
pH 7.5, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.27
1-Methylxanthine
pH 7.5, 30°C
3.17
Caffeine
pH 7.5, 30°C
2.17
paraxanthine
pH 7.5, 30°C
1.38
theophylline
pH 7.5, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
1-Methylxanthine
pH 7.5, 30°C
85.7
Caffeine
pH 7.5, 30°C
40.9
paraxanthine
pH 7.5, 30°C
151.6
theophylline
pH 7.5, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme forms part of the degradation pathway of methylxanthines
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NDMA_PSEPU
351
0
40203
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
x * 40000, SDS-PAGE
40200
x * 40200, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tagged fusion protein, expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Summers, R.M.; Louie, T.M.; Yu, C.L.; Subramanian, M.
Characterization of a broad-specificity non-haem iron N-demethylase from Pseudomonas putida CBB5 capable of utilizing several purine alkaloids as sole carbon and nitrogen source
Microbiology
157
583-592
2011
Pseudomonas putida (H9N289), Pseudomonas putida CBB5 (H9N289)
Manually annotated by BRENDA team
Summers, R.M.; Louie, T.M.; Yu, C.L.; Gakhar, L.; Louie, K.C.; Subramanian, M.
Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids
J. Bacteriol.
194
2041-2049
2012
Pseudomonas putida (H9N289), Pseudomonas putida CBB5 (H9N289)
Manually annotated by BRENDA team