Protein Variants | Comment | Organism |
---|---|---|
K174A | mutation of active site catalytic residue Lys174 to Ala results in a 20fold drop in the value of kcat, the Lys174Ala produces an unusual reverse-prenylated product, 3a-(2-methylbut-3-en-2-yl)-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole-2-carboxylic acid | Aspergillus fumigatus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
dimethylallyl diphosphate + L-tryptophan | Aspergillus fumigatus | - |
diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus fumigatus | Q50EL0 | gene 4-DMATS | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
dimethylallyl diphosphate + L-tryptophan = diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan | SN1-like mechanism involving a discrete carbocation intermediate involving initial ion pair formation followed by a reverse prenylation at the nucleophilic C-3 position, detailed overview | Aspergillus fumigatus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
dimethylallyl diphosphate + L-tryptophan | - |
Aspergillus fumigatus | diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan | - |
? | |
dimethylallyl diphosphate + L-tryptophan | the enzyme prenylates the non-nucleophilic C-4 position of the indole ring in free tryptophan | Aspergillus fumigatus | diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan | - |
? |
Synonyms | Comment | Organism |
---|---|---|
4-DMATS | - |
Aspergillus fumigatus |
FgaPT2 | - |
Aspergillus fumigatus |
General Information | Comment | Organism |
---|---|---|
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 | Aspergillus fumigatus |
additional information | key active site residues are Glu89 and Lys174 | Aspergillus fumigatus |