Formation of a stable and catalytically active complex of the two essential components of hexaprenyl diphosphate synthase from Micrococcus luteus B-P 26.
Formation of a stable complex of the two essential components of hexaprenyl diphosphate synthase from Micrococcus luteus B-P 26, which represents the catalytically active state of this enzyme, is observed in the presence of a relatively high concentrations of inorganic pyrophosphate or one of the substrates, isopentenyl diphosphate or farnesyl diphosphate. The apparent molecular mass of the complex is estimated to be about 50 kDa by gel filtration with Superose 12.
Yoshida
I
I
Chemical Research Institute of Non-Aqeous Solutions, Tohoku University, Sendai, Japan.
Koyama
T
T
Ogura
K
K
D019883:Alkyl and Aryl Transferases; D002384:Catalysis; D002850:Chromatography, Gel; D004122:Dimethylallyltranstransferase / Q000302:isolation & purification / Q000378:metabolism*; D011756:Diphosphates; D004795:Enzyme Stability; D045782:Hemiterpenes; D046911:Macromolecular Substances; D008837:Micrococcus / Q000201:enzymology*; D009943:Organophosphorus Compounds; D011106:Polyisoprenyl Phosphates; D012717:Sesquiterpenes; D013379:Substrate Specificity; D014166:Transferases / Q000378:metabolism*
D011756:Diphosphates; D045782:Hemiterpenes; D046911:Macromolecular Substances; D009943:Organophosphorus Compounds; D011106:Polyisoprenyl Phosphates; D012717:Sesquiterpenes; C004809:isopentenyl pyrophosphate; C004808:farnesyl pyrophosphate; D014166:Transferases; D019883:Alkyl and Aryl Transferases; D004122:Dimethylallyltranstransferase; C036826:trans-pentaprenyltranstransferase