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Literature summary for 2.5.1.34 extracted from

  • Mahmoodi, N.; Qian, Q.; Luk, L.; Tanner, M.
    Rearrangements in the mechanisms of the indole alkaloid prenyltransferases (2013), Pure Appl. Chem., 85, 1935-1948.
No PubMed abstract available
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Protein Variants

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/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dimethylallyl diphosphate + L-tryptophan Aspergillus fumigatus
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 diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan
-
 ?

Organism

Organism UniProt Comment Textmining
Aspergillus fumigatus Q50EL0 gene 4-DMATS
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Reaction

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
a

Substrates and Products (Substrate)

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

Synonyms Comment Organism
4-DMATS
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 Aspergillus fumigatus
FgaPT2
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 Aspergillus fumigatus

General Information

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