| Literature DB >> 17046541 |
Maki Fujiwara1, Jun-ichi Sumitani, Shinji Koga, Issei Yoshioka, Takuji Kouzuma, Shigeyuki Imamura, Takashi Kawaguchi, Motoo Arai.
Abstract
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).Entities:
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Year: 2006 PMID: 17046541 DOI: 10.1263/jbb.102.241
Source DB: PubMed Journal: J Biosci Bioeng ISSN: 1347-4421 Impact factor: 2.894