KEGG   ENZYME: 1.14.13.128
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
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)
R07965 R07966
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
ec00232  Caffeine metabolism
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
ec01120  Microbial metabolism in diverse environments
Orthology
K21724  7-methylxanthine demethylase
Genes
PCAF: DSC91_007652
MMS: mma_3678
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 157:583-92 (2011)
DOI:10.1099/mic.0.043612-0
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 194:2041-9 (2012)
DOI:10.1128/JB.06637-11
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.14.13.128
IUBMB Enzyme Nomenclature: 1.14.13.128
ExPASy - ENZYME nomenclature database: 1.14.13.128
UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.128
BRENDA, the Enzyme Database: 1.14.13.128
LinkDB

DBGET integrated database retrieval system