Fujiwara Maki, Sumitani Jun-ichi, Koga Shinji, Yoshioka Issei, Kouzuma Takuji, Imamura Shigeyuki, Kawaguchi Takashi, Arai Motoo
Department of Applied Life Sciences, Graduate School of Life and Environmental Sciences, Osaka Prefecture University, Sakai, Osaka, Japan.
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。
