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Literature summary for 1.5.8.2 extracted from
- pH and deuterium isotope effects on the reaction of trimethylamine dehydrogenase with dimethylamine (2019), Arch. Biochem. Biophys., 676, 108136 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methylophilus methylotrophus | P16099 | - |
- |
| Methylophilus methylotrophus W3A1 | P16099 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| TMD | - |
Methylophilus methylotrophus |
| TMDH | - |
Methylophilus methylotrophus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | the neutral amine of the substrate binds productively at the pH optimum. The deuterium (kcat/Kamine) value decreases to unity as the pH decreases, suggesting the presence of an alternative pathway at low pH, in which the protonated substrate binds and is then deprotonated by an active-site residue prior to oxidation. The kcat and deuterium kcat values both decrease to limiting values at low pH with similar pKa values. Above pH 10, the relative values of the two isotope effects establish that amine oxidation is about 4 times faster than a subsequent step or steps | Methylophilus methylotrophus |
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