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 |
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 |
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 |
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 |
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 | - |
? |
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 | - |
- |
- |
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 |
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 | - |
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 | ? | - |
? |
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 |
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 |
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 |
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 |