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Literature summary for extracted from

  • Metzger, U.; Schall, C.; Zocher, G.; Unsoeld, I.; Stec, E.; Li, S.M.; Heide, L.; Stehle, T.
    The structure of dimethylallyl tryptophan synthase reveals a common architecture of aromatic prenyltransferases in fungi and bacteria (2009), Proc. Natl. Acad. Sci. USA, 106, 14309-14314.
    View publication on PubMedView publication on EuropePMC


Cloned (Comment) Organism
expressed as a His-tagged fusion protein Aspergillus fumigatus

Crystallization (Commentary)

Crystallization (Comment) Organism
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


Organism UniProt Comment Textmining
Aspergillus fumigatus

Purification (Commentary)

Purification (Comment) Organism
using Ni-NTA chromatography Aspergillus fumigatus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dimethylallyl S-thiolodiphosphate + L-tryptophan dimethylallyl S-thiolodiphosphate serves as an analogue to the natural substrate, dimethylallyl diphosphate Aspergillus fumigatus ?


Synonyms Comment Organism
dimethylallyltryptophan synthase
Aspergillus fumigatus
Aspergillus fumigatus