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Literature summary extracted from

  • Yu, X.; Li, S.M.
    Prenyltransferases of the dimethylallyltryptophan synthase superfamily (2012), Methods Enzymol., 516, 259-278.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.5.1.B31 synthesis prenyltransferases of the DMATS superfamily are successfully used for production of prenylated compounds including analogues of their natural substrates such as simple indoles, tryptophan-containing cyclic dipeptides, and tyrosine derivatives, overview Claviceps purpurea
2.5.1.B31 synthesis prenyltransferases of the DMATS superfamily are successfully used for production of prenylated compounds including analogues of their natural substrates such as simple indoles, tryptophan-containing cyclic dipeptides, and tyrosine derivatives, overview Aspergillus fumigatus
2.5.1.B31 synthesis prenyltransferases of the DMATS superfamily are successfully used for production of prenylated compounds including analogues of their natural substrates such as simple indoles, tryptophan-containing cyclic dipeptides, and tyrosine derivatives, overview Malbranchea aurantiaca
2.5.1.34 synthesis prenyltransferases of the DMATS superfamily are successfully used for production of prenylated compounds including analogues of their natural substrates such as simple indoles, tryptophan-containing cyclic dipeptides, and tyrosine derivatives, overview Claviceps purpurea
2.5.1.34 synthesis prenyltransferases of the DMATS superfamily are successfully used for production of prenylated compounds including analogues of their natural substrates such as simple indoles, tryptophan-containing cyclic dipeptides, and tyrosine derivatives, overview Aspergillus fumigatus
2.5.1.34 synthesis prenyltransferases of the DMATS superfamily are successfully used for production of prenylated compounds including analogues of their natural substrates such as simple indoles, tryptophan-containing cyclic dipeptides, and tyrosine derivatives, overview Malbranchea aurantiaca
2.5.1.80 drug development 7-DMATS catalyzes regio- and stereospecific prenylations and can be used as efficient catalysts for chemoenzymatic synthesis of prenylated compounds, which can be then tested for their biological activities in drug discovery and development programs Aspergillus fischeri
2.5.1.80 drug development 7-DMATS catalyzes regio- and stereospecific prenylations and can be used as efficient catalysts for chemoenzymatic synthesis of prenylated compounds, which can be then tested for their biological activities in drug discovery and development programs Aspergillus clavatus
2.5.1.80 synthesis 7-DMATS catalyzes regio- and stereospecific prenylations and can be used as efficient catalysts for chemoenzymatic synthesis of prenylated compounds Aspergillus fischeri
2.5.1.80 synthesis 7-DMATS catalyzes regio- and stereospecific prenylations and can be used as efficient catalysts for chemoenzymatic synthesis of prenylated compounds Aspergillus clavatus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.B31 5-DMATS, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strains BL21, XL1 Blue, or M15 or in Saccharomyces cerevisiae strain INVSc1 Claviceps purpurea
2.5.1.B31 5-DMATS, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strains BL21, XL1 Blue, or M15 or in Saccharomyces cerevisiae strain INVSc1 Aspergillus fumigatus
2.5.1.B31 5-DMATS, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strains BL21, XL1 Blue, or M15 or in Saccharomyces cerevisiae strain INVSc1 Malbranchea aurantiaca
2.5.1.34 expression of His-tagged 4-DMATS in Escherichia coli strains XL1 Blue or M15 or in Saccharomyces cerevisiae strain INVSc1 Claviceps purpurea
2.5.1.34 expression of His-tagged 4-DMATS in Escherichia coli strains XL1 Blue or M15 or in Saccharomyces cerevisiae strain INVSc1 Aspergillus fumigatus
2.5.1.34 expression of His-tagged 4-DMATS in Escherichia coli strains XL1 Blue or M15 or in Saccharomyces cerevisiae strain INVSc1 Malbranchea aurantiaca
2.5.1.80 expression of His-tagged 7-DMATS in Escherichia coli strains XL1 Blue or M15 or in Saccharomyces cerevisiae strain INVSc1 Aspergillus fischeri
2.5.1.80 expression of His-tagged 7-DMATS in Escherichia coli strains XL1 Blue or M15 or in Saccharomyces cerevisiae strain INVSc1 Aspergillus clavatus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.B31 additional information
-
 additional information kinetics analysis, overview Claviceps purpurea
2.5.1.B31 additional information
-
 additional information kinetics analysis, overview Aspergillus fumigatus
2.5.1.B31 additional information
-
 additional information kinetics analysis, overview Malbranchea aurantiaca
2.5.1.34 additional information
-
 additional information kinetics analysis, overview Claviceps purpurea
2.5.1.34 additional information
-
 additional information kinetics analyis, overview Aspergillus fumigatus
2.5.1.34 additional information
-
 additional information kinetics analyis, overview Malbranchea aurantiaca
2.5.1.80 additional information
-
 additional information kinetics analyis, overview Aspergillus fischeri
2.5.1.80 additional information
-
 additional information kinetics analyis, overview Aspergillus clavatus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.5.1.B31 Ca2+ required Claviceps purpurea
2.5.1.B31 Ca2+ required Aspergillus fumigatus
2.5.1.B31 Ca2+ required Malbranchea aurantiaca
2.5.1.34 Ca2+ required Claviceps purpurea
2.5.1.34 Ca2+ required Aspergillus fumigatus
2.5.1.34 Ca2+ required Malbranchea aurantiaca
2.5.1.80 Ca2+ required Aspergillus fischeri
2.5.1.80 Ca2+ required Aspergillus clavatus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.B31 dimethylallyl diphosphate + L-tryptophan Claviceps purpurea
-
 diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 dimethylallyl diphosphate + L-tryptophan Aspergillus fumigatus
-
 diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 dimethylallyl diphosphate + L-tryptophan Malbranchea aurantiaca
-
 diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 additional information Claviceps purpurea 5-DMATS catalyzes prenylation of L-tryptophan at C-5 of the indole ring ?
-
 ?
2.5.1.B31 additional information Aspergillus fumigatus 5-DMATS catalyzes prenylation of L-tryptophan at C-5 of the indole ring ?
-
 ?
2.5.1.B31 additional information Malbranchea aurantiaca 5-DMATS catalyzes prenylation of L-tryptophan at C-5 of the indole ring ?
-
 ?
2.5.1.34 dimethylallyl diphosphate + L-tryptophan Claviceps purpurea
-
 diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.34 dimethylallyl diphosphate + L-tryptophan Aspergillus fumigatus
-
 diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.34 dimethylallyl diphosphate + L-tryptophan Malbranchea aurantiaca
-
 diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.34 additional information Claviceps purpurea DmaW catalyzes prenylation of L-tryptophan at C-4 of the indole ring and function as 4-DMATS ?
-
 ?
2.5.1.34 additional information Aspergillus fumigatus FgaPT2 catalyzes prenylation of L-tryptophan at C-4 of the indole ring and function as 4-DMATS ?
-
 ?
2.5.1.34 additional information Malbranchea aurantiaca MaPT catalyzes prenylation of L-tryptophan at C-4 of the indole ring and function as 4-DMATS ?
-
 ?
2.5.1.80 dimethylallyl diphosphate + L-tryptophan Aspergillus fischeri
-
 diphosphate + 7-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.80 dimethylallyl diphosphate + L-tryptophan Aspergillus clavatus
-
 diphosphate + 7-(3-methylbut-2-enyl)-L-tryptophan
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.B31 Aspergillus fumigatus
-
-
-
2.5.1.B31 Claviceps purpurea
-
-
-
2.5.1.B31 Malbranchea aurantiaca
-
-
-
2.5.1.34 Aspergillus fumigatus
-
-
-
2.5.1.34 Claviceps purpurea
-
-
-
2.5.1.34 Malbranchea aurantiaca
-
-
-
2.5.1.80 Aspergillus clavatus
-
-
-
2.5.1.80 Aspergillus fischeri
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.B31 recombinant His-tagged 5-DMATS from Escherichia coli strain BL21 or Saccharomyces cerevisiae strain INVSc1 by nickel affinity chromatography Claviceps purpurea
2.5.1.B31 recombinant His-tagged 5-DMATS from Escherichia coli strain BL21 or Saccharomyces cerevisiae strain INVSc1 by nickel affinity chromatography Aspergillus fumigatus
2.5.1.B31 recombinant His-tagged 5-DMATS from Escherichia coli strain BL21 or Saccharomyces cerevisiae strain INVSc1 by nickel affinity chromatography Malbranchea aurantiaca
2.5.1.34 recombinant His-tagged 4-DMATS from Escherichia coli strain BL21 or Saccharomyces cerevisiae strain INVSc1 by nickel affinity chromatography Claviceps purpurea
2.5.1.34 recombinant His-tagged 4-DMATS from Escherichia coli strain BL21 or Saccharomyces cerevisiae strain INVSc1 by nickel affinity chromatography Aspergillus fumigatus
2.5.1.34 recombinant His-tagged 4-DMATS from Escherichia coli strain BL21 or Saccharomyces cerevisiae strain INVSc1 by nickel affinity chromatography Malbranchea aurantiaca
2.5.1.80 recombinant His-tagged 7-DMATS from Escherichia coli strains XL1 Blue or M15 or from Saccharomyces cerevisiae strain INVSc1 by nickel affinity chromatography Aspergillus fischeri
2.5.1.80 recombinant His-tagged 7-DMATS from Escherichia coli strains XL1 Blue or M15 or from Saccharomyces cerevisiae strain INVSc1 by nickel affinity chromatography Aspergillus clavatus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.5.1.B31 mycelium
-
 Aspergillus fumigatus
-
2.5.1.34 mycelium
-
 Aspergillus fumigatus
-
2.5.1.80 mycelium
-
 Aspergillus clavatus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.B31 dimethylallyl diphosphate + L-tryptophan
-
 Claviceps purpurea diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 dimethylallyl diphosphate + L-tryptophan
-
 Aspergillus fumigatus diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 dimethylallyl diphosphate + L-tryptophan
-
 Malbranchea aurantiaca diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 additional information 5-DMATS catalyzes prenylation of L-tryptophan at C-5 of the indole ring Claviceps purpurea ?
-
 ?
2.5.1.B31 additional information 5-DMATS catalyzes prenylation of L-tryptophan at C-5 of the indole ring Aspergillus fumigatus ?
-
 ?
2.5.1.B31 additional information 5-DMATS catalyzes prenylation of L-tryptophan at C-5 of the indole ring Malbranchea aurantiaca ?
-
 ?
2.5.1.34 dimethylallyl diphosphate + L-tryptophan
-
 Claviceps purpurea diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.34 dimethylallyl diphosphate + L-tryptophan
-
 Aspergillus fumigatus diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.34 dimethylallyl diphosphate + L-tryptophan
-
 Malbranchea aurantiaca diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.34 additional information DmaW catalyzes prenylation of L-tryptophan at C-4 of the indole ring and function as 4-DMATS Claviceps purpurea ?
-
 ?
2.5.1.34 additional information FgaPT2 catalyzes prenylation of L-tryptophan at C-4 of the indole ring and function as 4-DMATS Aspergillus fumigatus ?
-
 ?
2.5.1.34 additional information MaPT catalyzes prenylation of L-tryptophan at C-4 of the indole ring and function as 4-DMATS Malbranchea aurantiaca ?
-
 ?
2.5.1.80 dimethylallyl diphosphate + L-tryptophan
-
 Aspergillus fischeri diphosphate + 7-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.80 dimethylallyl diphosphate + L-tryptophan
-
 Aspergillus clavatus diphosphate + 7-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.80 dimethylallyl diphosphate + L-tryptophan 7-DMATS accept L-tryptophan as substrate and prenylate it at C-7 Aspergillus fischeri diphosphate + 7-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.80 dimethylallyl diphosphate + L-tryptophan 7-DMATS accept L-tryptophan as substrate and prenylate it at C-7 Aspergillus clavatus diphosphate + 7-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.80 additional information 7-DMATS catalyzes regio- and stereospecific prenylations, assay conditions with different substrates, detailed overview Aspergillus fischeri ?
-
 ?
2.5.1.80 additional information 7-DMATS catalyzes regio- and stereospecific prenylations, assay conditions with different substrates, detailed overview Aspergillus clavatus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.5.1.B31 5-DMATS
-
 Claviceps purpurea
2.5.1.B31 5-DMATS
-
 Aspergillus fumigatus
2.5.1.B31 5-DMATS
-
 Malbranchea aurantiaca
2.5.1.34 4-DMATS
-
 Claviceps purpurea
2.5.1.34 4-DMATS
-
 Aspergillus fumigatus
2.5.1.34 4-DMATS
-
 Malbranchea aurantiaca
2.5.1.34 DmaW
-
 Claviceps purpurea
2.5.1.34 FgaPT2
-
 Aspergillus fumigatus
2.5.1.34 MaPT
-
 Malbranchea aurantiaca
2.5.1.80 7-DMATS
-
 Aspergillus fischeri
2.5.1.80 7-DMATS
-
 Aspergillus clavatus
2.5.1.80 dimethylallyltryptophan synthase
-
 Aspergillus fischeri
2.5.1.80 dimethylallyltryptophan synthase
-
 Aspergillus clavatus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.5.1.B31 30 37 assay at Claviceps purpurea
2.5.1.B31 30 37 assay at Aspergillus fumigatus
2.5.1.B31 30 37 assay at Malbranchea aurantiaca
2.5.1.34 30 37 assay at Claviceps purpurea
2.5.1.34 30 37 assay at Aspergillus fumigatus
2.5.1.34 30 37 assay at Malbranchea aurantiaca
2.5.1.80 30 37 assay at Aspergillus fischeri
2.5.1.80 30 37 assay at Aspergillus clavatus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.B31 7.5
-
 assay at Claviceps purpurea
2.5.1.B31 7.5
-
 assay at Aspergillus fumigatus
2.5.1.B31 7.5
-
 assay at Malbranchea aurantiaca
2.5.1.34 7.5
-
 assay at Claviceps purpurea
2.5.1.34 7.5
-
 assay at Aspergillus fumigatus
2.5.1.34 7.5
-
 assay at Malbranchea aurantiaca
2.5.1.80 7.5
-
 assay at Aspergillus fischeri
2.5.1.80 7.5
-
 assay at Aspergillus clavatus

General Information

EC Number General Information Comment Organism
2.5.1.B31 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 Claviceps purpurea
2.5.1.B31 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 Aspergillus fumigatus
2.5.1.B31 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 Malbranchea aurantiaca
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 Claviceps purpurea
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 Aspergillus fumigatus
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 Malbranchea aurantiaca
2.5.1.80 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 Aspergillus fischeri
2.5.1.80 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 Aspergillus clavatus