来自链格孢属菌株JS-103的果糖基氨基酸氧化酶底物特异性的改变。
Alteration of substrate specificity of fructosyl-amino acid oxidase from Ulocladium sp. JS-103.
作者信息
Fujiwara Maki, Sumitani Jun-ichi, Koga Shinji, Yoshioka Issei, Kouzuma Takuji, Imamura Shigeyuki, Kawaguchi Takashi, Arai Motoo
机构信息
Department of Applied Life Sciences, Graduate School of Life and Environmental Sciences, Osaka Prefecture University, Sakai, Osaka, Japan.
出版信息
J Biosci Bioeng. 2006 Sep;102(3):241-3. doi: 10.1263/jbb.102.241.
We showed by random mutagenesis that one-amino-acid substitution at Arg94 in fructosyl-amino acid oxidase from Ulocladium sp. JS-103 enhanced substrate specificity toward fructosyl valine (FV), a model compound of hemoglobin A(1c). Kinetic analysis showed that the specificity of the R94W mutant enzyme toward FV was 14-fold that of the wild-type enzyme. The mutant enzyme obtained will be useful in developing an enzymatic measurement method for hemoglobin A(1c).
我们通过随机诱变表明，来自链格孢属菌株JS-103的果糖基氨基酸氧化酶中第94位精氨酸的单氨基酸取代增强了对果糖基缬氨酸（FV）的底物特异性，FV是血红蛋白A1c的模型化合物。动力学分析表明，R94W突变酶对FV的特异性是野生型酶的14倍。所获得的突变酶将有助于开发一种用于血红蛋白A1c的酶促测量方法。
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