tailieunhanh - Báo cáo khoa học: An alternative mechanism of product chain-length determination in type III geranylgeranyl diphosphate synthase

(All-E) prenyl diphosphate synthases catalyze the con-secutive condensation of isopentenyl diphosphates with allylic prenyl diphosphates, producing products with vari-ous chain-lengths that are unique for each enzyme. Some short-chain (all-E) prenyl diphosphate synthases, . farnesyl diphosphate synthases and geranylgeranyl diphosphate synthases contain characteristic amino acid sequences around the allylic substrate binding sites, which have been shown to play a role in determining the chain-length of the product | Eur. J. Biochem. 270 2186-2194 2003 FEBS 2003 doi An alternative mechanism of product chain-length determination in type III geranylgeranyl diphosphate synthase Hisashi Hemmi Motoyoshi Noike Toru Nakayama and Tokuzo Nishino Department of Biomolecular Engineering Graduate School of Engineering Tohoku University Sendai Miyagi Japan All-E prenyl diphosphate synthases catalyze the consecutive condensation of isopentenyl diphosphates with allylic prenyl diphosphates producing products with various chain-lengths that are unique for each enzyme. Some short-chain all-E prenyl diphosphate synthases . farnesyl diphosphate synthases and geranylgeranyl diphosphate synthases contain characteristic amino acid sequences around the allylic substrate binding sites which have been shown to play a role in determining the chainlength of the product. However among these enzymes which are classified into several types based on the possessive patterns of such characteristics type III geranylgeranyl diphosphate synthases which consist of enzymes from eukaryotes excepting plants lack these features. In this study we report that mutagenesis at the second position before the conserved G Q E motif which is distant from the well-studied region affects the chainlength of the product for a type III geranylgeranyl diphosphate synthase from Saccharomyces cerevisiae. This clearly suggests that a novel mechanism is operative in the product determination for this type of enzyme. We also show herein that mutagenesis at the corresponding position of an archaeal medium-chain enzyme also alters its product specificity. These results provide valuable information on the molecular evolution of all-E prenyl diphosphate synthases. Keywords prenyltransferase geranylgeranyl diphosphate synthase hexaprenyl diphosphate synthase mutagenesis molecular evolution. All-E prenyl diphosphate synthases catalyze consecutive condensations of isopentenyl diphosphate IPP in the E-type .

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