EC Number | Cloned (Comment) | Organism |
---|---|---|
1.14.13.128 | expressed in Escherichia coli BL21(DE3) cells | Pseudomonas putida |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.14.13.128 | 0.0153 | - |
7-methylxanthine | in 50 mM potassium phosphate buffer (pH 7.5) at 30°C | Pseudomonas putida |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.14.13.128 | Iron | contains a non-heme iron domain | Pseudomonas putida |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.13.128 | 7-methylxanthine + O2 + NADH + H+ | Pseudomonas putida | the N7-demethylation reaction absolutely requires a unique, tightly bound protein complex composed of NdmC, NdmD, and NdmE. NdmE functions as a noncatalytic subunit that serves a structural role in the complexation of the oxygenase (NdmC) and Rieske domains (NdmD) | xanthine + NAD+ + H2O + formaldehyde | - |
? | |
1.14.13.128 | 7-methylxanthine + O2 + NADH + H+ | Pseudomonas putida CBB5 | the N7-demethylation reaction absolutely requires a unique, tightly bound protein complex composed of NdmC, NdmD, and NdmE. NdmE functions as a noncatalytic subunit that serves a structural role in the complexation of the oxygenase (NdmC) and Rieske domains (NdmD) | xanthine + NAD+ + H2O + formaldehyde | - |
? | |
1.14.13.128 | additional information | Pseudomonas putida | no activity toward caffeine or theobromine | ? | - |
? | |
1.14.13.128 | additional information | Pseudomonas putida CBB5 | no activity toward caffeine or theobromine | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.13.128 | Pseudomonas putida | M1EY73 | - |
- |
1.14.13.128 | Pseudomonas putida CBB5 | M1EY73 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.14.13.128 | Ni-NTA column chromatography and Sephacryl S200 gel filtration | Pseudomonas putida |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.13.128 | 7-methylxanthine + O2 + NADH + H+ | the N7-demethylation reaction absolutely requires a unique, tightly bound protein complex composed of NdmC, NdmD, and NdmE. NdmE functions as a noncatalytic subunit that serves a structural role in the complexation of the oxygenase (NdmC) and Rieske domains (NdmD) | Pseudomonas putida | xanthine + NAD+ + H2O + formaldehyde | - |
? | |
1.14.13.128 | 7-methylxanthine + O2 + NADH + H+ | the N7-demethylation reaction absolutely requires a unique, tightly bound protein complex composed of NdmC, NdmD, and NdmE. NdmE functions as a noncatalytic subunit that serves a structural role in the complexation of the oxygenase (NdmC) and Rieske domains (NdmD) | Pseudomonas putida CBB5 | xanthine + NAD+ + H2O + formaldehyde | - |
? | |
1.14.13.128 | additional information | no activity toward caffeine or theobromine | Pseudomonas putida | ? | - |
? | |
1.14.13.128 | additional information | no activity toward caffeine or theobromine | Pseudomonas putida CBB5 | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.13.128 | NdmC | - |
Pseudomonas putida |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.14.13.128 | 0.16 | - |
7-methylxanthine | in 50 mM potassium phosphate buffer (pH 7.5) at 30°C | Pseudomonas putida |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.13.128 | NADH | - |
Pseudomonas putida |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.14.13.128 | 10.17 | - |
7-methylxanthine | in 50 mM potassium phosphate buffer (pH 7.5) at 30°C | Pseudomonas putida |