A non-heme iron oxygenase. The enzyme from the bacterium Pseudomonas putida shares an NAD(P)H-FMN reductase subunit with EC 1.14.13.179, methylxanthine N3-demethylase, and has a 5-fold higher activity with NADH than with NADPH . Also demethylate 1-methylxantine with lower efficiency. Forms part of the degradation pathway of methylxanthines.
Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
caffeine:oxygen oxidoreductase (N1-demethylating)
A non-heme iron oxygenase. The enzyme from the bacterium Pseudomonas putida shares an NAD(P)H-FMN reductase subunit with EC 1.14.13.179, methylxanthine N3-demethylase, and has a 5-fold higher activity with NADH than with NADPH [2]. Also demethylate 1-methylxantine with lower efficiency. Forms part of the degradation pathway of methylxanthines.
the enzyme forms part of the degradation pathway of methylxanthines. The activity of the enzyme is dependent on electron transfer from NADH via a redox-center-dense Rieske reductase, NdmD
the enzyme forms part of the degradation pathway of methylxanthines. The activity of the enzyme is dependent on electron transfer from NADH via a redox-center-dense Rieske reductase, NdmD
the enzyme forms part of the degradation pathway of methylxanthines. The activity of the enzyme is dependent on electron transfer from NADH via a redox-center-dense Rieske reductase, NdmD
the enzyme forms part of the degradation pathway of methylxanthines. The activity of the enzyme is dependent on electron transfer from NADH via a redox-center-dense Rieske reductase, NdmD
the enzyme forms part of the degradation pathway of methylxanthines. The activity of the enzyme is dependent on electron transfer from NADH via a redox-center-dense Rieske reductase, NdmD
the enzyme forms part of the degradation pathway of methylxanthines. The activity of the enzyme is dependent on electron transfer from NADH via a redox-center-dense Rieske reductase, NdmD
the enzyme forms part of the degradation pathway of methylxanthines. The activity of the enzyme is dependent on electron transfer from NADH via a redox-center-dense Rieske reductase, NdmD
the enzyme forms part of the degradation pathway of methylxanthines. The activity of the enzyme is dependent on electron transfer from NADH via a redox-center-dense Rieske reductase, NdmD
the enzyme forms part of the degradation pathway of methylxanthines. The activity of the enzyme is dependent on electron transfer from NADH via a redox-center-dense Rieske reductase, NdmD
the enzyme forms part of the degradation pathway of methylxanthines. The activity of the enzyme is dependent on electron transfer from NADH via a redox-center-dense Rieske reductase, NdmD
a reductase component with cytochrome c reductase activity transfers reducing equivalents from NAD(P)H to the enzyme. NADH is the preferred substrate of the reductase component. Activity with NADPH is 22% of that with NADH
a reductase component with cytochrome c reductase activity transfers reducing equivalents from NAD(P)H to the enzyme. NADH is the preferred substrate of the reductase component. Activity with NADPH is 22% of that with NADH
the soluble N-demethylase holoenzyme is composed of two components, a reductase component with cytochrome c reductase activity (Ccr) and a two-subunit N-demethylase component (Ndm). Ndm, with a native molecular mass of 240000 Da, is composed of NdmA (40000 Da) and NdmB (35000 Da). Ccr transfers reducing equivalents from NAD(P)H to Ndm, which catalyses an oxygen-dependent N-demethylation of methylxanthines to xanthine, formaldehyde and water
the soluble N-demethylase holoenzyme is composed of two components, a reductase component with cytochrome c reductase activity (Ccr) and a two-subunit N-demethylase component (Ndm). Ndm, with a native molecular mass of 240000 Da, is composed of NdmA (40000 Da) and NdmB (35000 Da). Ccr transfers reducing equivalents from NAD(P)H to Ndm, which catalyses an oxygen-dependent N-demethylation of methylxanthines to xanthine, formaldehyde and water
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
BRENDA home
History
Enzyme Nomenclature
1.14.13.178 methylxanthine N1-demethylase
top
