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Results 1 - 5 of 5
EC Number Reaction Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.1.2.10[protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3 - -
Display the word mapDisplay the reaction diagram Show all sequences 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
Display the word mapDisplay the reaction diagram Show all sequences 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
Display the word mapDisplay the reaction diagram Show all sequences 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
Display the word mapDisplay the reaction diagram Show all sequences 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
Results 1 - 5 of 5