EC Number   |
General Information |
Reference |
|---|
   2.5.1.34 | evolution |
4-DMATS follows a mechanism that involves initial ion pair formation followed by a reverse prenylation at the nucleophilic C-3 position. Generation of the C-4 normal prenylated intermediate and deprotonation rearomatizes the indole ring. The enzyme tryprostatin B synthase (FtmPT1) catalyzes the normal C-2 prenylation of the indole ring in brevianamide F (cyclo-L-Trp-L-Pro). It shares high structural homology with 4-DMATS, and catalyzes a reaction in favor of an initial C-3 prenylation (either normal or reverse) followed by carbo cation rearrangements to give product. The concept of a common intermediate that partitions to different products via rearrangements can help to explain how these evolutionarily related enzymes can prenylate different positions on the indole ring |
726466 |
| 2.5.1.34 | evolution |
all of the members of the structurally related dimethylallyltryptophan synthase family show a common mechanism for prenylation of tryptophan |
722461 |
| 2.5.1.34 | evolution |
collectively a family of enzymes, the dimethylallyl tryptophan synthases (DMATS) catalyze alkylation of the indole ring in tryptophan or tryptophan-containing dipeptides at positions N1, C2, C3, C4, C5, C6, or C7 by dimethylallyl diphosphate (DMAPP) to give the different naturally occurring carbon skeletons. The dimethylallyl moiety can be attached at C1' (normal prenylation) or C3' (reverse prenylation), further increasing structural diversity |
722461 |
| 2.5.1.34 | evolution |
FgaPT2 belongs to the DMATS superfamily |
721373 |
| 2.5.1.34 | evolution |
the enzyme belongs to the dimethylallyl-tryptophan synthase, DMATS, superfamily |
723326 |
| 2.5.1.34 | evolution |
the enzyme belongs to the DMATS superfamily. The members of the DMATS superfamily contain no DDxxD motifs, which are essential for binding of prenyl diphosphate via metal ions, for example, Mg2+ or Mn2+, in trans prenyltransferases |
723104 |
| 2.5.1.34 | evolution |
the enzyme is part of the DMATS superfamily |
737544, 739221 |
| 2.5.1.34 | evolution |
Trp-DMATS is capable of catalyzing prenylation without the requirement of Mg2+, a unique characteristic that distinguishes the Trp-DMATS family of prenyl transferases |
737837 |
| 2.5.1.34 | metabolism |
4-DMATS catalyzes the first step in the biosynthesis of ergot alkaloids |
721293 |
| 2.5.1.34 | metabolism |
4-DMATS catalyzes the normal prenylation of tryptophan at C4 by DMAPP as the first committed step in ergot alkaloid biosynthesis |
722461 |
