Phân tích tư tưởng của nhân dân qua đoạn thơ: Những người vợ nhớ chồng… Những cuộc đời đã hóa sông núi ta trong Đất nước của Nguyễn Khoa Điềm
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Y238, oneof thevery fewconservedresidues in theactive siteofD-amino acid oxidases (DAAO), was mutated to phe-nylalanine and serine in the enzyme from the yeastRhodo-torula gracilis. The mutated proteins are catalyticallycompetent thus eliminating Tyr238 as an active-site acid/base catalyst. Y238FandY238Smutants exhibit a threefoldslower turnover on D-alanine as substrate, which can beattributed to a slower rate of product release relative to thewild-type enzyme (a change of the rate constants for sub-strate binding was also evident). ...
Nội dung trích xuất từ tài liệu:
Báo cáo Y học: Role of tyrosine 238 in the active site of Rhodotorula gracilis D-amino acid oxidase A site-directed mutagenesis study
