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evolution
all of the members of the structurally related dimethylallyltryptophan synthase family show a common mechanism for prenylation of tryptophan
evolution
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FgaPT2 belongs to the DMATS superfamily
evolution
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the enzyme belongs to the dimethylallyl-tryptophan synthase, DMATS, superfamily
evolution
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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
evolution
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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
evolution
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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
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
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
evolution
the enzyme is part of the DMATS superfamily
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
metabolism
4-DMATS catalyzes the normal prenylation of tryptophan at C4 by DMAPP as the first committed step in ergot alkaloid biosynthesis
metabolism
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4-DMATS catalyzes the first step in the biosynthesis of ergot alkaloids
metabolism
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the enzyme catalyzes the first step of ergot alkaloid biosynthesis
metabolism
dimethylallyltryptophan synthases (DMATSs) catalyze regiospecific transfer reactions of a prenyl moiety from dimethylallyl diphosphate to various positions of the indole ring of tryptophan. The 4-DMATS enzyme FgaPT2 is involved in biosynthesis of fumigaclavine C
metabolism
the enzyme is involved in the biosynthesis of fumigaclavine C
metabolism
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inactivation of this gene does not prevent the production of roquefortine C
metabolism
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the enzyme is involved in biosynthesis of isofumigaclavine A
metabolism
the enzyme is involved is in the biosynthesis of the ergot alkaloids fumigaclavines
metabolism
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the enzyme is involved is in the biosynthesis of the ergot alkaloids fumigaclavines
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metabolism
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inactivation of this gene does not prevent the production of roquefortine C
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metabolism
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the enzyme is involved in biosynthesis of isofumigaclavine A
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physiological function
the aromatic prenyltransferase dimethylallyltryptophan synthase in Claviceps purpurea catalyzes the normal prenylation of tryptophan at C4 of the indole nucleus in the first committed step of ergot alkaloid biosynthesis
physiological function
FgaPT2 plays a role in the first pathway-specific enzyme during ergot alkaloids biosynthesis and catalyzes the regular prenylation of L-tryptophan at the C4 position
additional information
comparison of the three-dimensional structural models of 7-DMATSNeo from Neosartorya sp. with FgaPT2 (4-DMATS) from Aspergillus fumigatus
additional information
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comparison of the three-dimensional structural models of 7-DMATSNeo from Neosartorya sp. with FgaPT2 (4-DMATS) from Aspergillus fumigatus
additional information
key active site residues are Glu89 and Lys174
additional information
possibility of producing prenylated analogues of ardeemin fumiquinazoline, a precursor of the multidrug resistance (MDR) export pump inhibitor ardeemin, by using dimethylallydiphosphate transferase enzymes, e.g. 4-DMATS, docking study of FgaPT2 with ardeemin fumiquinazoline and its stereoisomers, overview