Any feedback?
No. of entries
Information on EC 1.14.13.178 - methylxanthine N1-demethylase
for references in articles please use BRENDA:EC1.14.13.178
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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
1.14.13.178 methylxanthine N1-demethylase
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.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
show+
+
+
=
+
+
+
Synonyms
methylxanthine n1-demethylase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ndmA
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
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
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
caffeine degradation I (main, plants), caffeine degradation III (bacteria, via demethylation), theophylline degradation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-methylxanthine + O2 + NADH + H+
xanthine + NAD+ + H2O + formaldehyde
Substrates: -
Products: -
Products: -
?
paraxanthine + O2 + NADH + H+
7-methylxanthine + NAD+ + H2O + formaldehyde
Substrates: -
Products: -
Products: -
?
theophylline + O2 + NADPH + H+
3-methylxanthine + NADP+ + H2O + formaldehyde
-
Substrates: i.e. 1,3-dimethylxanthine
Products: -
Products: -
?
caffeine + O2 + NAD(P)H + H+
theobromine + NAD(P)+ + H2O + formaldehyde
Substrates: -
Products: -
Products: -
?
caffeine + O2 + NAD(P)H + H+
theobromine + NAD(P)+ + H2O + formaldehyde
Substrates: 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
Products: -
Products: -
?
caffeine + O2 + NAD(P)H + H+
theobromine + NAD(P)+ + H2O + formaldehyde
Substrates: -
Products: -
Products: -
?
caffeine + O2 + NAD(P)H + H+
theobromine + NAD(P)+ + H2O + formaldehyde
Substrates: 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
Products: -
Products: -
?
caffeine + O2 + NADH + H+
theobromine + NAD+ + H2O + formaldehyde
Substrates: the activity of the enzyme is dependent on electron transfer from NADH via a redox-center-dense Rieske reductase, NdmD
Products: -
Products: -
?
caffeine + O2 + NADH + H+
theobromine + NAD+ + H2O + formaldehyde
Substrates: the activity of the enzyme is dependent on electron transfer from NADH via a redox-center-dense Rieske reductase, NdmD
Products: -
Products: -
?
paraxanthine + O2 + NAD(P)H + H+
7-methylxanthine + NAD(P)+ + H2O + formaldehyde
Substrates: -
Products: -
Products: -
?
paraxanthine + O2 + NAD(P)H + H+
7-methylxanthine + NAD(P)+ + H2O + formaldehyde
Substrates: 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
Products: -
Products: -
?
paraxanthine + O2 + NAD(P)H + H+
7-methylxanthine + NAD(P)+ + H2O + formaldehyde
Substrates: -
Products: -
Products: -
?
paraxanthine + O2 + NAD(P)H + H+
7-methylxanthine + NAD(P)+ + H2O + formaldehyde
Substrates: 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
Products: -
Products: -
?
theophylline + O2 + NAD(P)H + H+
3-methylxanthine + NAD(P)+ + H2O + formaldehyde
Substrates: -
Products: -
Products: -
?
theophylline + O2 + NAD(P)H + H+
3-methylxanthine + NAD(P)+ + H2O + formaldehyde
Substrates: 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
Products: -
Products: -
?
theophylline + O2 + NAD(P)H + H+
3-methylxanthine + NAD(P)+ + H2O + formaldehyde
Substrates: -
Products: -
Products: -
?
theophylline + O2 + NADH + H+
3-methylxanthine + NAD+ + H2O + formaldehyde
Substrates: -
Products: -
Products: -
?
theophylline + O2 + NADH + H+
3-methylxanthine + NAD+ + H2O + formaldehyde
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with theobromine, 3-methylxanthine and 7-methylxanthine
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with theobromine, 3-methylxanthine and 7-methylxanthine
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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
Substrates: 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
Products: -
Products: -
?
theophylline + O2 + NADPH + H+
3-methylxanthine + NADP+ + H2O + formaldehyde
-
Substrates: i.e. 1,3-dimethylxanthine
Products: -
Products: -
?
caffeine + O2 + NAD(P)H + H+
theobromine + NAD(P)+ + H2O + formaldehyde
Substrates: 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
Products: -
Products: -
?
caffeine + O2 + NAD(P)H + H+
theobromine + NAD(P)+ + H2O + formaldehyde
Substrates: 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
Products: -
Products: -
?
paraxanthine + O2 + NAD(P)H + H+
7-methylxanthine + NAD(P)+ + H2O + formaldehyde
Substrates: 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
Products: -
Products: -
?
paraxanthine + O2 + NAD(P)H + H+
7-methylxanthine + NAD(P)+ + H2O + formaldehyde
Substrates: 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
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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.
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.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease 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.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A2S6TW62_9PROT
291
0
32983
TrEMBL
-
A0A399FDJ8_9DEIN
320
0
36223
TrEMBL
-
A0A177H7V9_9RHOB
214
0
23928
TrEMBL
-
A0A1V5P5F8_9CHLR
331
0
37767
TrEMBL
-
A0A5E6MHM9_9BACT
321
0
36117
TrEMBL
-
A0A5A5RSZ2_MICAE
446
2
51920
TrEMBL
-
A0A1V5VUY4_9CHLR
293
0
33287
TrEMBL
-
A0A5A5RJT7_MICAE
446
2
52119
TrEMBL
-
A0A347WB90_9PROT
218
0
23736
TrEMBL
-
A0A645D0W2_9ZZZZ
327
0
35976
TrEMBL
other Location (Reliability: 2)
A0A290LJR1_9BURK
356
0
40696
TrEMBL
-
A0A6J5FNC4_9BURK
356
0
40696
TrEMBL
-
A0A1J5RUJ8_9ZZZZ
359
0
40998
TrEMBL
Mitochondrion (Reliability: 5)
B1FSR2_PARG4
Paraburkholderia graminis (strain ATCC 700544 / DSM 17151 / LMG 18924 / NCIMB 13744 / C4D1M)
344
0
39930
TrEMBL
-
A0A346BIK8_9BURK
359
0
39997
TrEMBL
-
A0A5K6CVM1_ACIB3
Acinetobacter baumannii (strain AB307-0294)
351
0
39975
TrEMBL
-
A0A347WG69_9PROT
351
0
39380
TrEMBL
-
A0A6J5GC38_9BURK
351
0
39486
TrEMBL
-
A0A5E6MFD4_9BACT
348
0
38524
TrEMBL
-
A0A347WFI7_9PROT
346
0
39380
TrEMBL
-
A0A402DDB6_MICAE
446
2
51986
TrEMBL
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
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.
SUBUNIT
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.
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)
brenda
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)
brenda
Sarkar, M.; Hunt, C.; Guzelian, P.; Karnes, H.
Characterization of human liver cytochromes P-450 involved in theophylline metabolism
Drug Metab. Dispos.
20
31-37
1992
Homo sapiens
brenda
EXTERNAL LINKS (specific for EC-Number 1.14.13.178)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
