To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...]
View this page in https

ENZYME entry: EC 1.14.13.179

Accepted Name
Methylxanthine N(3)-demethylase.
Reaction catalysed
  • Theobromine + O(2) + NAD(P)H <=> 7-methylxanthine + NAD(P)(+) + H(2)O + formaldehyde
  • 3-methylxanthine + O(2) + NAD(P)H <=> xanthine + NAD(P)(+) + H(2)O + formaldehyde
Cofactor(s)
Fe cation.
Comment(s)
  • The enzyme from the bacterium Pseudomonas putida shares an NAD(P)H-FMN reductase subunit with EC 1.14.13.178, and has higher activity with NADH than with NADPH.
  • Also demethylates caffeine and theophylline with lower efficiency.
  • Forms part of the degradation pathway of methylxanthines.
Cross-references
BRENDA1.14.13.179
EC2PDB1.14.13.179
ExplorEnz1.14.13.179
PRIAM enzyme-specific profiles1.14.13.179
KEGG Ligand Database for Enzyme Nomenclature1.14.13.179
IUBMB Enzyme Nomenclature1.14.13.179
IntEnz1.14.13.179
MEDLINEFind literature relating to 1.14.13.179
MetaCyc1.14.13.179
UniProtKB/Swiss-Prot
H9N290, NDMB_PSEPU

View entry in original ENZYME format
View entry in raw text format (no links)

All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.13.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-