1.14.13.128: 7-methylxanthine demethylase
This is an abbreviated version!
For detailed information about 7-methylxanthine demethylase, go to the full flat file.
Word Map on EC 1.14.13.128
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1.14.13.128
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putida
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demethylation
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theophylline
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bioreactors
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uric
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coffee
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trimethyl
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costly
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1,3,7-trimethylxanthine
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rhodococcus
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paraxanthine
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3,7-dimethylxanthine
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formaldehyde
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aminopyrine
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alcaligenes
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rieske
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broad-specificity
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non-heme
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3-methylxanthine
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oxygen-dependent
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methylxanthines
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commences
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bioprocess
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klebsiella
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pharmacology
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medicine
- 1.14.13.128
- putida
-
demethylation
- theophylline
-
bioreactors
-
uric
- coffee
-
trimethyl
-
costly
- 1,3,7-trimethylxanthine
- rhodococcus
- paraxanthine
- 3,7-dimethylxanthine
- formaldehyde
- aminopyrine
- alcaligenes
-
rieske
-
broad-specificity
-
non-heme
- 3-methylxanthine
-
oxygen-dependent
- methylxanthines
-
commences
-
bioprocess
- klebsiella
- pharmacology
- medicine
Reaction
Synonyms
7-methylxanthine-specific N-demethylase, bacterial N-demethylase, caffeine demethylase, heteroxanthine demethylase, methylxanthine N-demethylase, N-demethylase, ndmA, NdmC, theobromine demethylase
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General Information on EC 1.14.13.128 - 7-methylxanthine demethylase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
metabolism
physiological function
additional information
based on the sequence of a genomic fragment, caffeine demethylation enzyme system found in Pseudomonas sp. is predicted to consist of a two-component Rieske monooxygenases namely NdmA and NdmB specific towards methyl groups at 1 and 3 positions in xanthine ring respectively and one kind of three-component Rieske monooxygenase system comprising a monooxygenase NdmC specific towards 7-methylxanthine, a reductase component NdmD and a structural protein NdmE. NdmD also acts as the reductase component for NdmA and NdmB. The Rieske domain present in NdmD serves to function as an electron transfer domain during catalysis by NdmC as it lacks its own Rieske domain. NdmC forms a large multi-subunit complex comprising 2 monomeric units of each NdmC, NdmD, and NdmE and follows the typical electron flow pattern of Rieske oxygenases. The N-terminal Rieske domain found in NdmD is a product of domain shuffling between NdmC and NdmD during evolution and is not required for its reductase activity
evolution
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catabolism of caffeine in microorganisms commences via two possible mechanisms: demethylation and oxidation. Through the demethylation route, the major metabolite formed in fungi is theophylline, whereas theobromine is the major metabolite in bacteria
evolution
the N-terminal Rieske domain found in NdmD is a product of domain shuffling between NdmC and NdmD during evolution and is not required for its reductase activity
metabolism
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catabolism of caffeine in microorganisms commences via two possible mechanisms: demethylation and oxidation. Through the demethylation route, the major metabolite formed in fungi is theophylline, whereas theobromine is the major metabolite in bacteria. Catabolism of caffeine in microorganisms, overview
metabolism
Rieske nonheme iron oxygenases (ROs) catalyze the initial oxygenation reaction of aromatic compounds by enantio- and regiospecific reactions. The type of RO in Pseudomonas putida strain CBB5, consists of NdmA, NdmB, and NdmC, which specifically detach methyl groups from the N-1, N-3, and N-7 positions of methylxanthine derivatives, respectively. A single formaldehyde is produced whenever one N-linked methyl group is detached, indicating that NdmA, NdmB, and NdmC are monooxygenases.The N-demethylation of caffeine to xanthine occurs via three steps; NdmA and NdmB catalyze the initial two steps of N-demethylation, and the intermediate product, 7-methylxanthine, is further catalyzed to xanthine by an unusual RO-reductase complex, the NdmCDE heterotrimer. Heterohexamerization of NdmA and NdmB under physiological conditions. NdmD is the RO reductase that forms a stable ternary complex with NdmC and NdmE (NdmCDE). Since NdmC detaches the N-7 methyl group from methylxanthine derivatives, the NdmCDE complex is responsible for the last N-demethylation step of caffeine to xanthine. But NdmD is also needed by both NdmA and NdmB for electron transport from NADH to the oxygen activation site. Therefore, it is expected that transient interaction would exist between them. Electron transfer pathway from the ferredoxin domain of NdmD to caffeine in the catalytic site of NdmA. Enzyme complex structure analysis structure-function analysis, overview
metabolism
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Rieske nonheme iron oxygenases (ROs) catalyze the initial oxygenation reaction of aromatic compounds by enantio- and regiospecific reactions. The type of RO in Pseudomonas putida strain CBB5, consists of NdmA, NdmB, and NdmC, which specifically detach methyl groups from the N-1, N-3, and N-7 positions of methylxanthine derivatives, respectively. A single formaldehyde is produced whenever one N-linked methyl group is detached, indicating that NdmA, NdmB, and NdmC are monooxygenases.The N-demethylation of caffeine to xanthine occurs via three steps; NdmA and NdmB catalyze the initial two steps of N-demethylation, and the intermediate product, 7-methylxanthine, is further catalyzed to xanthine by an unusual RO-reductase complex, the NdmCDE heterotrimer. Heterohexamerization of NdmA and NdmB under physiological conditions. NdmD is the RO reductase that forms a stable ternary complex with NdmC and NdmE (NdmCDE). Since NdmC detaches the N-7 methyl group from methylxanthine derivatives, the NdmCDE complex is responsible for the last N-demethylation step of caffeine to xanthine. But NdmD is also needed by both NdmA and NdmB for electron transport from NADH to the oxygen activation site. Therefore, it is expected that transient interaction would exist between them. Electron transfer pathway from the ferredoxin domain of NdmD to caffeine in the catalytic site of NdmA. Enzyme complex structure analysis structure-function analysis, overview
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physiological function
the enzyme NdmA catalyzes NADH-dependent N1-demethylation of caffeine to theobromine and theophylline to 3-methylxanthine, and subsequently to 7-methylxanthine, and xanthine. The oxidoreductase NdmD, UniProt ID H9N291, catalyzes the oxidation of NADH and transfers electrons to NdmA and NdmB, which catalyze the N-demethylation reaction
physiological function
Pseudomonas sp. NCIM 5235 is a caffeine-degrading bacterial strain that metabolizes caffeine by sequential demethylation using methylxanthine demethylases, including 7-methylxanthine demethylase NdmC. These enzymes belong to the class of two-component Rieske oxygenases and require an oxidoreductase, NdmD, for efficient catalysis. Three oxygenases (NdmA, NdmB, and NdmC) specific towards methyl groups at 1, 3, and 7 positions in xanthine ring share a common reductase component, NdmD, analysis of NdmD parameters and function, overview. Another structural protein and oxidoreductase NdmE has also been shown to be required for catalysis by NdmC. Rieske oxygenases are an important class of enzymes that have been reported to play a major role in the degradation of xenobiotic compounds and drugs
physiological function
some bacteria, such as Pseudomonas putida strain CBB5, utilize caffeine as a sole carbon and nitrogen source by degrading it through sequential N-demethylation catalyzed by five enzymes: NdmA, NdmB, NdmC, NdmD, and NdmE. Enzyme NdmC specifically detaches methyl groups from the N-7 position of methylxanthine derivatives, NdmC is a monooxygenase
physiological function
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the enzyme NdmA catalyzes NADH-dependent N1-demethylation of caffeine to theobromine and theophylline to 3-methylxanthine, and subsequently to 7-methylxanthine, and xanthine. The oxidoreductase NdmD, UniProt ID H9N291, catalyzes the oxidation of NADH and transfers electrons to NdmA and NdmB, which catalyze the N-demethylation reaction
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physiological function
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some bacteria, such as Pseudomonas putida strain CBB5, utilize caffeine as a sole carbon and nitrogen source by degrading it through sequential N-demethylation catalyzed by five enzymes: NdmA, NdmB, NdmC, NdmD, and NdmE. Enzyme NdmC specifically detaches methyl groups from the N-7 position of methylxanthine derivatives, NdmC is a monooxygenase
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