Product chain-length determination mechanism of Z,E-farnesyl diphosphate synthase |
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Authors: | Noike Motoyoshi Ambo Takanori Kikuchi Sayaka Suzuki Toshihide Yamashita Satoshi Takahashi Seiji Kurokawa Hirofumi Mahapatra Sebabrata Crick Dean C Koyama Tanetoshi |
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Affiliation: | a Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, Katahira 2-1-1, Aoba-ku, Sendai, Miyagi 980-8577, Japan b Department of Microbiology, Immunology, and Pathology, College of Veterinary Medicine and Biomedical Sciences, Colorado State University, 1682 Campus Delivery, Fort Collins, CO 80523-1682, USA |
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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. |
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Keywords: | IPP isopentenyl diphosphate GPP geranyl diphosphate CITPP citronellyl diphosphate E E-FPP E E-farnesyl diphosphate Z E-FPP Z E-farnesyl diphosphate GGPP geranylgeranyl diphosphate DedolPS dehydrodolichyl diphosphate synthase HDS human dehydrodolichyl diphosphate synthase |
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