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.
Research Article|February 01 1986
A novel prenyltransferase from Paracoccus denitrificans
Biochem J (1986) 233 (3): 773-777.
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K Ishii, H Sagami, K Ogura; A novel prenyltransferase from Paracoccus denitrificans. Biochem J 1 February 1986; 233 (3): 773–777. doi: https://doi.org/10.1042/bj2330773
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