Product chain-length determination mechanism of Z,E-farnesyl diphosphate synthase.
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Noike M, Ambo T, Kikuchi S, Suzuki T, Yamashita S, Takahashi S, Kurokawa H, Mahapatra S, Crick DC, Koyama T
Product chain-length determination mechanism of Z,E-farnesyl diphosphate synthase.
Biochem Biophys Res Commun. 2008 Dec 5;377(1):17-22. doi: 10.1016/j.bbrc.2008.09.014. Epub 2008 Sep 13.
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- 18790692 [ View in PubMed]
- Abstract
cis-Prenyltransferases catalyze the consecutive condensation of isopentenyl diphosphate (IPP) with allylic prenyl diphosphates, producing Z,E-mixed prenyl diphosphate. The Mycobacterium tuberculosis Z,E-farnesyl diphosphate synthase Rv1086 catalyzes the condensation of one molecule of IPP with geranyl diphosphate to yield Z,E-farnesyl diphosphate and is classified as a short-chain cis-prenyltransferase. To elucidate the chain-length determination mechanism of the short-chain cis-prenyltransferase, we introduced some substitutive mutations at the characteristic amino acid residues of Rv1086. Among the mutants constructed, L84A showed a dramatic change of catalytic function to synthesize longer prenyl chain products than that of wild type, indicating that Leu84 of Rv1086 plays an important role in product chain-length determination. Mutagenesis at the corresponding residue of a medium-chain cis-prenyltransferase, Micrococcus luteus B-P 26 undecaprenyl diphosphate synthase also resulted in the production of different prenyl chain length from the intrinsic product, suggesting that this position also plays an important role in product chain-length determination for medium-chain cis-prenyltransferases.