| Budget Amount *help |
¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2014: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2013: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2012: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Outline of Final Research Achievements |
Polyhydroxyalkanoate (PHA) is important bacterial polyester that is degraded by specific enzymes in environment. In this study, structure and function relationships of enzymes in PHA metabolism were investigated for the sake of development of the design and synthetic system of new biopolyesters. A multi-domain PHA depolymerase was crystallized, and its crystal structure in complex with an oligomeric substrate was successfully determined. The results indicated a novel interaction mode between the PHA depolymerase with the type I catalytic domain and polymer substrate. In addition, a novel hydrolase which degrades a soluble polymer polyaspartate was successfully crystallized, and its crystal structure in complex with an oligomeric substrate were determined. The interaction mode between the enzyme and the substrate indicated similarity with that of a fungal PHA depolymerase with the type II catalytic domain.
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