Any feedback?
Literature summary for 2.5.1.34 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 |
|---|---|
| expression of His-tagged 4-DMATS in Escherichia coli strains XL1 Blue or M15 or in Saccharomyces cerevisiae strain INVSc1 | Claviceps purpurea |
| expression of His-tagged 4-DMATS in Escherichia coli strains XL1 Blue or M15 or in Saccharomyces cerevisiae strain INVSc1 | Aspergillus fumigatus |
| expression of His-tagged 4-DMATS in Escherichia coli strains 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 analyis, overview | Aspergillus fumigatus | |
| additional information | - |
additional information | kinetics analyis, 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 + 4-(3-methylbut-2-enyl)-L-tryptophan | - |
? | |
| dimethylallyl diphosphate + L-tryptophan | Aspergillus fumigatus | - |
diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan | - |
? | |
| dimethylallyl diphosphate + L-tryptophan | Malbranchea aurantiaca | - |
diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan | - |
? | |
| additional information | Claviceps purpurea | DmaW catalyzes prenylation of L-tryptophan at C-4 of the indole ring and function as 4-DMATS | ? | - |
? | |
| additional information | Aspergillus fumigatus | FgaPT2 catalyzes prenylation of L-tryptophan at C-4 of the indole ring and function as 4-DMATS | ? | - |
? | |
| additional information | Malbranchea aurantiaca | MaPT catalyzes prenylation of L-tryptophan at C-4 of the indole ring and function as 4-DMATS | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus fumigatus | - |
- |
- |
| Claviceps purpurea | - |
- |
- |
| Malbranchea aurantiaca | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged 4-DMATS from Escherichia coli strain BL21 or Saccharomyces cerevisiae strain INVSc1 by nickel affinity chromatography | Claviceps purpurea |
| recombinant His-tagged 4-DMATS from Escherichia coli strain BL21 or Saccharomyces cerevisiae strain INVSc1 by nickel affinity chromatography | Aspergillus fumigatus |
| recombinant His-tagged 4-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 + 4-(3-methylbut-2-enyl)-L-tryptophan | - |
? | |
| dimethylallyl diphosphate + L-tryptophan | - |
Aspergillus fumigatus | diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan | - |
? | |
| dimethylallyl diphosphate + L-tryptophan | - |
Malbranchea aurantiaca | diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan | - |
? | |
| additional information | DmaW catalyzes prenylation of L-tryptophan at C-4 of the indole ring and function as 4-DMATS | Claviceps purpurea | ? | - |
? | |
| additional information | FgaPT2 catalyzes prenylation of L-tryptophan at C-4 of the indole ring and function as 4-DMATS | Aspergillus fumigatus | ? | - |
? | |
| additional information | MaPT catalyzes prenylation of L-tryptophan at C-4 of the indole ring and function as 4-DMATS | Malbranchea aurantiaca | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 4-DMATS | - |
Claviceps purpurea |
| 4-DMATS | - |
Aspergillus fumigatus |
| 4-DMATS | - |
Malbranchea aurantiaca |
| DmaW | - |
Claviceps purpurea |
| FgaPT2 | - |
Aspergillus fumigatus |
| MaPT | - |
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 |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
