2001 Fiscal Year Final Research Report Summary
In vitro biosynthesis of enantiomeric ether polar lipids in Archaea
| Project/Area Number |
11460051
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
応用微生物学・応用生物化学
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| Research Institution | University of Occupational and Environmental Health |
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Principal Investigator |
KOGA Yosuke University of Occupational and Environmental Health, School of medicine. Professor, 医学部, 教授 (70012458)
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| Co-Investigator(Kenkyū-buntansha) |
MORII Hiroyuki University of Occupational and Environmental Health, School of Health Science, Assistant professor, 産業保健学部, 助手 (60141743)
NISHIHARA Masateru University of Occupational and Environmental Health, School of medicine, Associate professor, 医学部, 助教授 (20131930)
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| Project Period (FY) |
1999 – 2001
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| Keywords | ether lipid / phospholipid biosynthesis / sn-glycerol-1-phosphate / CDP-archaeol synthase / archaetidylserine synthase |
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| Research Abstract |
The most fundamental characteristics. that distinguishes Archaea from Bacteria/Eucarya is membrane ether-type polar lipids, especially their sn-glycerol-1-phosphate (G-1-P) backbone. G-1-P dehydrogenase, which is the key enzyme for the formation of lipid G-1-P backbone, was found ubiquitously in several species of Archaea including methanogens, hyperthermophiles, an acidothermophile, and an extreme halophile as far as analysed. The gene (egsA) encoding the enzyme was also detected by homology search in all the Archaea whose genome sequences have been published. Archaeitidic acid, which is formed from DHAP by etherification with two geranylgeranyl groups, was in turn activated by CTP. The product is CDP-archaeol. The substrate specificities of CDP-archaeol synthase- and archetidylserine synthase were established in this study. CDP-archaeol synthase was specific to the substrate with geranylgeranyl groups as hydrocarbon chains. It did not recognized stereostructure of glycerophosphate backbone or ether bonds. AS synthase did not discriminate substrates with unsaturated and saturated hydrocarbons, ether bonds and ester bonds, or stereostructures of glycerophosphate backbone. The enzymatic properties of archaeal AS synthase were quite similar to Bacillus phosphatidylserine synthase except for the optimal temperature, and the amino acid sequences showed significant similarity. These results suggested archaeal AS synthase and bacterial phosphatidylserine synthase share their ancestor.
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