EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
  1.14.13.B34 | more |
enzyme NdmD shows broad substrate specificity with highest catalytic efficiency towards cytochrome c. The enzyme NdmD shows cytochrome c reductase (ccr, EC 1.1.1.2) activity towards three different substrates cytochrome c, DCPIP, and potassium ferricyanide,, kinetics overviews. NdmD also assists as an oxidoreductase the demethylase activity of NdmA, NdmB, and NdmC, overview. NdmD is the reductase component of the different methylxanthine demethylases. NdmD does not catalyze caffeine demethylation but only acts as a reductase |
Pseudomonas sp. NCIM 5235 |
? |
- |
- |
| 1.14.13.B34 | more |
the enzyme NdmD shows cytochrome c reductase (ccr, EC 1.1.1.2) activity. NdmD also is the RO reductase that forms a stable ternary complex with NdmC and NdmE (NdmCDE). Since NdmC detaches the N-7 methyl group from methylxanthine derivatives, the NdmCDE complex is responsible for the last N-demethylation step of caffeine to xanthine. But NdmD is also needed by both demethylases NdmA and NdmB for electron transport from NADH to the oxygen activation site, as a demethylase reductase. Therefore, it is expected that transient interaction would exist between them |
Pseudomonas putida |
? |
- |
- |
| 1.14.13.B34 | more |
the enzyme NdmD shows cytochrome c reductase (ccr, EC 1.1.1.2) activity. NdmD also is the RO reductase that forms a stable ternary complex with NdmC and NdmE (NdmCDE). Since NdmC detaches the N-7 methyl group from methylxanthine derivatives, the NdmCDE complex is responsible for the last N-demethylation step of caffeine to xanthine. But NdmD is also needed by both demethylases NdmA and NdmB for electron transport from NADH to the oxygen activation site, as a demethylase reductase. Therefore, it is expected that transient interaction would exist between them |
Pseudomonas putida CBB5 |
? |
- |
- |
