EC Number | Cloned (Comment) | Organism |
---|---|---|
2.5.1.34 | expressed as a His-tagged fusion protein | Aspergillus fumigatus |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.5.1.34 | x-ray structure of DMATS, determined at a resolution of 1.76 A is reported. A complex of DMATS with its substrate L-tryptophan and with an analogue of its isoprenoid substrate dimethylallyl diphosphate reveals the structural basis of this enzyme-catalyzed Friedel-Crafts reaction, showing strict regiospecificity for position 4 of the indole nucleus of tryptophan as well as unusual independence of the presence of Mg2+ ions. The 3D structure of DMATS belongs to a rare alpha/beta barrel fold, called prenyltransferase barrel, that is present in a small group of bacterial enzymes with no sequence similarity to DMATS | Aspergillus fumigatus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.5.1.34 | Aspergillus fumigatus | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.5.1.34 | using Ni-NTA chromatography | Aspergillus fumigatus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.5.1.34 | dimethylallyl S-thiolodiphosphate + L-tryptophan | dimethylallyl S-thiolodiphosphate serves as an analogue to the natural substrate, dimethylallyl diphosphate | Aspergillus fumigatus | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.5.1.34 | dimethylallyltryptophan synthase | - |
Aspergillus fumigatus |
2.5.1.34 | DMATS | - |
Aspergillus fumigatus |