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2.5.1.34: 4-dimethylallyltryptophan synthase

This is an abbreviated version!
For detailed information about 4-dimethylallyltryptophan synthase, go to the full flat file.

Word Map on EC 2.5.1.34

Reaction

dimethylallyl diphosphate
+
L-tryptophan
=
diphosphate
 +
4-(3-methylbut-2-enyl)-L-tryptophan

Synonyms

4-(gamma,gamma-dimethylallyl)tryptophan synthase, 4-dimethylallyltryptophan synthase, 4-DMATS, 7-dimethylallyltryptophan synthase, 7-DMATS, C4-prenyltransferase, dimethylallyl-tryptophan synthase, dimethylallylpyrophosphate:L-tryptophan dimethylallyltransferase, dimethylallylpyrophosphate:tryptophan dimethylallyl transferase, dimethylallylpyrophosphate:tryptophan dimethylallyltransferase, dimethylallyltransferase, tryptophan, dimethylallyltryptophan synthase, dimethylallyltryptophan synthetase, DMAT synthase, DMAT synthetase, DMATS, DmaW, DmaW2, FgaPT2, IfgA, MaPT, Proq05g069320, tryptophan C4-prenyltransferase, tryptophan C4-prenyltransferase FgaPT2, tryptophan C4-PT

ECTree

     2 Transferases
         2.5 Transferring alkyl or aryl groups, other than methyl groups
             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
                2.5.1.34 4-dimethylallyltryptophan synthase

Crystallization

Crystallization on EC 2.5.1.34 - 4-dimethylallyltryptophan synthase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis
the crystal structure of FgaPT2 (4-DMATS) is determined as a complex with its aromatic substrate L-tryptophan and with dimethylallyl S-thiolodiphosphate (DMSPP), an analogue of its isoprenoid substrate dimethylallyl diphosphate, X-ray structural analysis and three-dimensional structural modeling
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
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