2001 Fiscal Year Final Research Report Summary
Changes in the Substrate Specificities of Farnesyl Diphosphate Synthase by a Single Amino Acid Substitution
| Project/Area Number |
12680587
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Bioorganic chemistry
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| Research Institution | Yamagata University |
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Principal Investigator |
MAKI Yuji Yamagata University, Department of Material and Biological Chemistry, 理学部, 教授 (00007171)
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| Project Period (FY) |
2000 – 2001
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| Keywords | farnesyl diphosphate synthase / substrate analog / mutated enzyme / thermostable enzyme / geranyl diphosphate / dimethylallyl diphosphate / substrate specificity / isopentenyl diphosphate |
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| Research Abstract |
Farnesyl diphosphate (FPP) synthase catalyze the condensation of isopentenyl diphosphate (IPP) with allylic primer to give FPP as final product. The FPS from pig liver has been successfully applied to syntheses of bioactive compounds. Molecular cloning and expression of the gene for thermostable FPS from Bacillus stearothermophilus made it possible to produce sufficient amounts of the enzyme. However it can hardly accept the substrate analogs having oxygen atom in their chain, which are easily accepted by the pig the liver enzyme. There may be some limitations in the thermostable enzyme for applying to organic synthesis. We constructed the FPP syntheses (FPSs) from Bacillus stearothermophilus, in which Tyr-81 was substituted with Ser (S), Arg (R), Asp (D), or Gly (G). Interestingly the substrate specificities of the mutated enzymes have been dramatically altered. They can easily accept the substrate analogs having oxygen atom. These results may suggest the application of the prenyltransferases to organic synthesis is more available.
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