   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 |
