Product chain-length determination mechanism of Z,E-farnesyl diphosphate synthase

Motoyoshi Noike, Takanori Ambo, Sayaka Kikuchi, Toshihide Suzuki, Satoshi Yamashita, Seiji Takahashi, Hirofumi Kurokawa, Sebabrata Mahapatra, Dean C. Crick, Tanetoshi Koyama

研究成果: Article査読

15 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)17-22
ページ数6
ジャーナルBiochemical and biophysical research communications
377
1
DOI
出版ステータスPublished - 2008 12 5

ASJC Scopus subject areas

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

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