EC Number   |
Natural Substrates |
|---|
   2.5.1.34 | dimethylallyl diphosphate + L-tryptophan |
- |
| 2.5.1.34 | dimethylallyl diphosphate + L-tryptophan |
first pathway-specific enzyme of ergot alkaloid biosynthesis |
| 2.5.1.34 | dimethylallyl diphosphate + L-tryptophan |
first key step in ergot alkaloid biosynthesis providing the pharmaceutically relevant compounds lysergic acid, ergotamine, fumigaclavine A-C, festuclavine, and elymoclavine |
| 2.5.1.34 | dimethylallyl diphosphate + L-tryptophan |
dimethylallyltryptophan synthase catalyzes both normal and reverse prenylation at C3 of the indole ring and normal prenylation of N1 |
| 2.5.1.34 | dimethylallyl diphosphate + L-tryptophan |
C-4 prenylation |
| 2.5.1.34 | dimethylallyl diphosphate + L-tryptophan |
the enzyme is involved in the biosynthesis of the ergot alkaloids fumigaclavines |
| 2.5.1.34 | more |
DmaW catalyzes prenylation of L-tryptophan at C-4 of the indole ring and function as 4-DMATS |
| 2.5.1.34 | more |
FgaPT2 catalyzes prenylation of L-tryptophan at C-4 of the indole ring and function as 4-DMATS |
| 2.5.1.34 | more |
MaPT catalyzes prenylation of L-tryptophan at C-4 of the indole ring and function as 4-DMATS |
| 2.5.1.34 | more |
4-DMATS catalyzes normal prenylation at C4 of L-tryptophan. When C4 is blocked, 4-DMATS catalyzes alkylation at all of the activated positions, except weakly activated C6, depending on the electron-donating properties of the blocking substituent. In addition, both normal and reverse prenylation is seen at C3 for 4-methyltryptophan. The high regioselectivity for C4 alkylation with the normal substrates suggests that binding and catalysis of a single conformation has been optimized for synthesis of 4-dimethylallyltryptophan, but when alkylation at C4 is blocked, alkylation from other conformations becomes competitive |
