KEGG   ENZYME: 1.14.13.179Help
Entry
EC 1.14.13.179              Enzyme                                 

Name
methylxanthine N3-demethylase;
ndmB (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
theobromine:oxygen oxidoreductase (N3-demethylating)
Reaction(IUBMB)
(1) theobromine + O2 + NAD(P)H + H+ = 7-methylxanthine + NAD(P)+ + H2O + formaldehyde [RN:R07961 R07962];
(2) 3-methylxanthine + O2 + NAD(P)H + H+ = xanthine + NAD(P)+ + H2O + formaldehyde [RN:R07967 R07968]
Reaction(KEGG)
Substrate
theobromine [CPD:C07480];
O2 [CPD:C00007];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080];
3-methylxanthine [CPD:C16357]
Product
7-methylxanthine [CPD:C16353];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006];
H2O [CPD:C00001];
formaldehyde [CPD:C00067];
xanthine [CPD:C00385]
Comment
A non-heme iron oxygenase. The enzyme from the bacterium Pseudomonas putida shares an NAD(P)H-FMN reductase subunit with EC 1.14.13.178, methylxanthine N1-demethylase, and has higher activity with NADH than with NADPH [1]. Also demethylates caffeine and theophylline with lower efficiency. Forms part of the degradation pathway of methylxanthines.
History
EC 1.14.13.179 created 2013
Pathway
ec00232  Caffeine metabolism
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
ec01120  Microbial metabolism in diverse environments
Orthology
K21723  methylxanthine N3-demethylase
Genes
MMS: mma_0224
PYE: A6J80_10955
ASZ: ASN_2439(vanA)
Taxonomy
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
  Sequence
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: 1.14.13.179
IUBMB Enzyme Nomenclature: 1.14.13.179
ExPASy - ENZYME nomenclature database: 1.14.13.179
BRENDA, the Enzyme Database: 1.14.13.179

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