EC 1.14.13.179 - Methylxanthine N3-demethylase

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IntEnz Enzyme Nomenclature
EC 1.14.13.179

Names

Accepted name:
methylxanthine N3-demethylase
Other name:
ndmB (gene name)
Systematic name:
theobromine:oxygen oxidoreductase (N3-demethylating)

Reactions

Cofactor

Comments:

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.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Summers, R. M., Louie, T. M., Yu, C. L., Subramanian, M.
    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.
    Microbiology (Reading, Engl.) 157: 583-592 (2011). [PMID: 20966097]
  2. Summers, R. M., Louie, T. M., Yu, C. L., Gakhar, L., Louie, K. C., Subramanian, M.
    Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids.
    J. Bacteriol. 194: 2041-2049 (2012). [PMID: 22328667]

[EC 1.14.13.179 created 2013]