Báo cáo Y học: Role of tyrosine 238 in the active site of Rhodotorula gracilis D-amino acid oxidase A site-directed mutagenesis study
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Y238, oneof thevery fewconservedresidues in theactive site ofD-amino acid oxidases (DAAO), was mutated to phe-nylalanine and serine in the enzyme from the yeastRhodo-torula gracilis. The mutated proteins are catalytically competent thus eliminating Tyr238 as an active-site acid/ base catalyst. Y238FandY238Smutants exhibit a threefold slower turnover on D-alanine as substrate, which can be attributed to a slower rate of product release relative to the wild-type enzyme (a change of the rate constants for sub-strate binding was also evident). ...
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