EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.18.1.3 | 42000 | - |
gel filtration | Pseudomonas putida |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.15.26 | Pseudomonas putida | - |
- |
- |
1.18.1.3 | Pseudomonas putida | P21394 | enzyme acts as reductase component of xylene monooxygenase, EC 1.18.1.3 | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.18.1.3 | electron-transfer component XylA | Pseudomonas putida |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.18.1.3 | ? | x * 40000, SDS-PAGE | Pseudomonas putida |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.15.26 | xylM | - |
Pseudomonas putida |
1.18.1.3 | XYLA | - |
Pseudomonas putida |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.15.26 | additional information | electron-transfer component XylA, EC 1.18.1.3 contains 1 mol FAD per mol of enzyme. The electron flow is from NADH to FAD to[2Fe-2S] | Pseudomonas putida | |
1.18.1.3 | FAD | 1 mol/mol enzyme. The electron flow is from NADH to FAD to [2Fe-2S] | Pseudomonas putida | |
1.18.1.3 | NADH | electron-transfer component XylA. The electron flow is from NADH to FAD to [2Fe-2S] | Pseudomonas putida | |
1.18.1.3 | [2Fe-2S]-center | protein contains 2 mol/mol of non-haem iron and 2 mol/mol of acid-labile sulfide. The electron flow is from NADH to FAD to [2Fe-2S] | Pseudomonas putida |