| Project/Area Number |
12480169
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (B)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
Bioorganic chemistry
|
|---|
| Research Institution | TOHOKU UNIVERSITY |
|---|
Principal Investigator |
KOYAMA Tanetoshi Tohoku University, lnstitute of Multidisciplinary Research for Advanced Materials, Professor, 多元物質科学研究所, 教授 (20089808)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
YUAN-WEI Zhang Tohoku University, lnstitute of Maltidisciplinary Research for Advanced Materials, Research Associate, 多元物質科学研究所, 助手 (10302241)
OHYA Norimasa Yamagata University, Faculty of Science, Lecturer, 理学部, 講師 (40302286)
|
|---|
| Project Period (FY) |
2000 – 2002
|
| Keywords | PRENYL CHAIN ELONGATION / FARNESYL DIPHOSPHATE / UNDECAPRENYL DIPHOSPHATE / PRENYLTRANSFERASE / ISOPRENOID BIOSYNTHESIS / SUBSTRATE BINDING SITE / ENZYME STRUCTURE / SITE-DIRECTED MUTAGENESIS |
|---|
| Research Abstract |
In the biosynthesis of isoprenoid compounds all of the carbon backbones are derived from prenyl diphosphates, which are synthesized by the action of prenyltransferases.
During the last decades the structural genes for many kinds of prenyltransferases catalyzing (E)-type prenyl chain elongation have been identified and characterized. However, no information has been available about the structures of (Z)-prenyl diphosphate syntheses until our isolation of the gene for Micrococcus luteus undecaprenyl diphosphate synthase in 1998. The amino acid sequence of the (Z)-prenyl diphosphate synthase is totally different from those of (E)-prenyl chain elongating enzymes.
The crystal structure of the undecaprenyl diphosphate synthase has been determined at 2.2 A resolution as the first three dimensional structure among cis-prenyl chain elongating enzymes. This enzyme shows a novel protein fold which is completely different from those for the enzymes relating to isoprenoid biosynthesis, having a commo
… More
n structure "isoprenoid synthase fold". A plausible substrate-binding model of the enzyme has been deduced from the precise three-dimensional structure as well as the data accumulated from site-directed mutagenesis experiments.
We have isolated and characterized the cDNA for the rubber transferaes from Hevea brasiliensis. In viro rubber production using the recombinant enzyme overexpressed in E. coli cells revealed that the Hevea rubber transferase might require some activation factors in the washed bottom particle fraction of Hevea latex for the production of high molecular weight rubber molecules.
Dolichol has an essential role in the biosynthesis of N-linked glycoproteins and glycosylphosphatidylinositol-anchored proteins as the glycosyl carrier lipid in higher organisms. Through the database search for a gene encoding highly conserved regions for cis-prenyl chain elongating enzymes, we have identified a human dehydrodolichyl diphosphate synthase. The mRNA expression levels of the dehydrodolichyl diphosphate synthase in human tissues were analyzed by Northern blotting to show high expressions in testis as well as in kidney. Less
|
