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Literature summary for 2.5.1.B31 extracted from
- Prenyltransferases of the dimethylallyltryptophan synthase superfamily (2012), Methods Enzymol., 516, 259-278.
Application
| Application | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
| 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 |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| 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 |
| 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 |
| 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 |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics analysis, overview | Claviceps purpurea | |
| additional information | - |
additional information | kinetics analysis, overview | Aspergillus fumigatus | |
| additional information | - |
additional information | kinetics analysis, overview | Malbranchea aurantiaca |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | required | Claviceps purpurea |  |
| Ca2+ | required | Aspergillus fumigatus | |
| Ca2+ | required | Malbranchea aurantiaca | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| dimethylallyl diphosphate + L-tryptophan | Claviceps purpurea | - |
diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan | - |
? | |
| dimethylallyl diphosphate + L-tryptophan | Aspergillus fumigatus | - |
diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan | - |
? | |
| dimethylallyl diphosphate + L-tryptophan | Malbranchea aurantiaca | - |
diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan | - |
? | |
| additional information | Claviceps purpurea | 5-DMATS catalyzes prenylation of L-tryptophan at C-5 of the indole ring | ? | - |
? | |
| additional information | Aspergillus fumigatus | 5-DMATS catalyzes prenylation of L-tryptophan at C-5 of the indole ring | ? | - |
? | |
| additional information | Malbranchea aurantiaca | 5-DMATS catalyzes prenylation of L-tryptophan at C-5 of the indole ring | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus fumigatus | - |
- |
- |
| Claviceps purpurea | - |
- |
- |
| Malbranchea aurantiaca | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged 5-DMATS from Escherichia coli strain BL21 or Saccharomyces cerevisiae strain INVSc1 by nickel affinity chromatography | Claviceps purpurea |
| recombinant His-tagged 5-DMATS from Escherichia coli strain BL21 or Saccharomyces cerevisiae strain INVSc1 by nickel affinity chromatography | Aspergillus fumigatus |
| recombinant His-tagged 5-DMATS from Escherichia coli strain BL21 or Saccharomyces cerevisiae strain INVSc1 by nickel affinity chromatography | Malbranchea aurantiaca |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| mycelium | - |
Aspergillus fumigatus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| dimethylallyl diphosphate + L-tryptophan | - |
Claviceps purpurea | diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan | - |
? | |
| dimethylallyl diphosphate + L-tryptophan | - |
Aspergillus fumigatus | diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan | - |
? | |
| dimethylallyl diphosphate + L-tryptophan | - |
Malbranchea aurantiaca | diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan | - |
? | |
| additional information | 5-DMATS catalyzes prenylation of L-tryptophan at C-5 of the indole ring | Claviceps purpurea | ? | - |
? | |
| additional information | 5-DMATS catalyzes prenylation of L-tryptophan at C-5 of the indole ring | Aspergillus fumigatus | ? | - |
? | |
| additional information | 5-DMATS catalyzes prenylation of L-tryptophan at C-5 of the indole ring | Malbranchea aurantiaca | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 5-DMATS | - |
Claviceps purpurea |
| 5-DMATS | - |
Aspergillus fumigatus |
| 5-DMATS | - |
Malbranchea aurantiaca |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 37 | assay at | Claviceps purpurea |
| 30 | 37 | assay at | Aspergillus fumigatus |
| 30 | 37 | assay at | Malbranchea aurantiaca |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Claviceps purpurea |
| 7.5 | - |
assay at | Aspergillus fumigatus |
| 7.5 | - |
assay at | Malbranchea aurantiaca |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
| 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 |
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