Alteration of substrate specificity of fructosyl-amino acid oxidase from Ulocladium sp. JS-103
| Autor: | Shigeyuki Imamura, Takuji Kouzuma, Jun-ichi Sumitani, Maki Fujiwara, Issei Yoshioka, Motoo Arai, Shinji Koga, Takashi Kawaguchi |
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| Rok vydání: | 2006 |
| Předmět: |
Mutation
Missense Bioengineering Biology medicine.disease_cause Applied Microbiology and Biotechnology Substrate Specificity Fungal Proteins Ascomycota Valine medicine Humans Glycated Hemoglobin chemistry.chemical_classification Mutation Oxidase test Mutagenesis biology.organism_classification Enzyme Hemoglobin A Amino Acid Substitution Biochemistry chemistry Biological Assay Amino Acid Oxidoreductases Hemoglobin Biotechnology Ulocladium |
| Zdroj: | Journal of Bioscience and Bioengineering. 102:241-243 |
| ISSN: | 1389-1723 |
| DOI: | 10.1263/jbb.102.241 |
| Popis: | 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). |
| Databáze: | OpenAIRE |
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