Structure-function studies of metabolic enzymes for design of novel biodegradable biopolymers

2014 Fiscal Year Final Research Report

• Project/Area Number: 24510114
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Environmental technology/Environmental materials
• Research Institution: The Institute of Physical and Chemical Research
• Principal Investigator: HISANO Tamao 独立行政法人理化学研究所, 放射光科学総合研究センター, 専任研究員 (20312267)
• Project Period (FY): 2012-04-01 – 2015-03-31
• Keywords: 環境調和型材料 / バイオポリエステル / 生分解性高分子 / 微生物酵素 / 構造と機能 / 結晶構造解析

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.

Free Research Field

構造生物学