A novel prenyltransferase from Paracoccus denitrificans.
A new polyprenyltransferase catalysing the formation of Z-double bonds was found and partially purified from extracts of Paracoccus denitrificans. The enzyme catalysed a consecutive condensation of isopentenyl diphosphate with EE-farnesyl diphosphate as a primer to produce EE-farnesyl-all-Z-hexaprenyl diphosphate (ZE-mixed nonaprenyl diphosphate) as the final product. Not only EE-farnesyl diphosphate but also neryl diphosphate, ZE-farnesyl diphosphate, ZEE-geranylgeranyl diphosphate and ZZEE-pentaprenyl diphosphate were all accepted as substrates. This polyprenyltransferase required detergent such as Triton X-100 for its catalytic activity. The formation of ZE-mixed undecaprenyl diphosphate, which is well known as the precursor of the bacterial sugar-carrier lipid, was not detected in extracts of this bacterium.
Ishii
K
K
Sagami
H
H
Ogura
K
K
D000135:Acid Phosphatase / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D002853:Chromatography, Liquid; D004122:Dimethylallyltranstransferase / Q000302:isolation & purification* / Q000378:metabolism; D045782:Hemiterpenes; D009943:Organophosphorus Compounds / Q000378:metabolism; D010231:Paracoccus denitrificans / Q000201:enzymology*; D013379:Substrate Specificity; D014166:Transferases / Q000302:isolation & purification*
D045782:Hemiterpenes; D009943:Organophosphorus Compounds; C004809:isopentenyl pyrophosphate; D014166:Transferases; D004122:Dimethylallyltranstransferase; D000135:Acid Phosphatase