EC Number |
Reaction |
Reference |
---|
2.1.2.10 | [protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3 |
- |
- |
2.1.2.10 | [protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3 |
5-methyltetrahydrofolate is bound in a kinked shape with the pteridine group deeply buried into the hydrophobic pocket ant the glutamyl group pointed to the C-terminal side surface. R292 interacts through water molecules with the folate polyglutamate tail |
662653 |
2.1.2.10 | [protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3 |
formation of a folate-binding cavity via the interaction of enzyme with H-protein |
662123 |
2.1.2.10 | [protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3 |
T-protein recognition of lipoyl protein substrate and reaction mechanism, overview. The reversible transfer of the methylene group between the lipoate and tetrahydrofolate proceeds through the electron relay-assisted iminium intermediate formation |
719865 |
2.1.2.10 | [protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3 |
tetrahydrofolate is bound near the center of the tripartite enzyme, lipoic acid is bound adjacent to the tetrahydrofolate binding pocket |
662303 |