生体触媒の新しい機能・特性の探索と解析

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In this paper, I describe the molecular and functional characterizations of three distinct biocatalysts of biotechnological interest for the purpose of showing that they are interesting examples of the functional and structural differentiation of enzymes within protein families. These biocatalysts are the Saccharo-polyspora rectivirgula β-galactosidase (srbg) of the glycosyl hydrolase family 2, the Bacillus sp. SAM 1606 α-glucosidase of the glycosyl hydrolase family 13, and the Antirrhinum majus aureusidin synthase (AmAS 1) of the plant polyphenol oxidase family. These biocatalysts were found to be clearly distinct from other members of each family, mainly in terms of subunit structure and metal ion requirements (for srbg), substrate specificity and transglucosylation activity (for SAM 1606 α-glucosidase), and biological function (for AmAS 1). Extensive analyses of such unique properties and functions through protein and genetic engineering approaches provided important information for insights into the molecular and functional evolution of each protein family.
社団法人日本生物工学会の論文
2002-03-25