KEGG   ENZYME: 1.14.13.128Help
Entry
EC 1.14.13.128              Enzyme                                 

Name
7-methylxanthine demethylase;
ndmC (gene name)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy
Sysname
7-methylxanthine:oxygen oxidoreductase (demethylating)
Reaction(IUBMB)
7-methylxanthine + O2 + NAD(P)H + H+ = xanthine + NAD(P)+ + H2O + formaldehyde [RN:R07965 R07966]
Reaction(KEGG)
Substrate
7-methylxanthine [CPD:C16353];
O2 [CPD:C00007];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Product
xanthine [CPD:C00385];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006];
H2O [CPD:C00001];
formaldehyde [CPD:C00067]
Comment
A non-heme iron oxygenase. The enzyme from the bacterium Pseudomonas putida prefers NADH over NADPH. The enzyme is specific for 7-methylxanthine [2]. Forms part of the caffeine degradation pathway.
History
EC 1.14.13.128 created 2011
Pathway
Caffeine metabolism
Microbial metabolism in diverse environments
Reference
1  [PMID:20966097]
  Authors
Summers RM, Louie TM, Yu CL, Subramanian M
  Title
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.
  Journal
Microbiology. 157 (2011) 583-92.
Reference
2  [PMID:22328667]
  Authors
Summers RM, Louie TM, Yu CL, Gakhar L, Louie KC, Subramanian M
  Title
Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids.
  Journal
J. Bacteriol. 194 (2012) 2041-9.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
UM-BBD (Biocatalysis/Biodegradation Database): 
BRENDA, the Enzyme Database: 

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