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Title 

Purification and Characterization of the 2-ketoaldonate reductase from Brevibacterium ketosoreductum ATCC21914

Authors 

Do Young YumSung Sook BaeJae Gu Pan

Publisher 

Japan Society for Bioscience, Biotechnology and Agrochemistry

Issue Date 

1998

Citation 

Bioscience Biotechnology and Biochemistry, vol. 62, no. 1, pp. 154-156

Keywords 

2-ketoaldonate reductaseBrevibacterium ketosoreductumketogluconate metabolism

Abstract 

2-Ketoaldonate reductase, which is involved in ketogluconate catabolism, was purified to homogeneity from Brevibacterium ketosoreductum ATCC21914. The enzyme was found to catalyze the reduction of 2,5-diketo-D-gluconate to 5-keto-D-gluconate, and to a lesser extent, 2-keto-D-gluconate to D-gluconate, and 2-keto-L-gluconate to L-idonate. The molecular mass of the reductase was 35 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 72 kDa by gel filtration, indicating that the native enzyme may exist as a dimer. The reductase was optimally active at pH 6.0 with NADPH as a preferred electron donor. The pI of 4.7 was measured for the enzyme. The apparent Km for 2,5-diketo-D-gluconate and NADPH were 5 microM and 10 microM, respectively. The amino-terminal amino acid sequence was NH2-Ala-Ser-Ile-Ser-Val-Ser-Val-Pro-Ser-Ala- Arg-Leu-Ala-Glu-Asp-Leu-Ser-Asp-Ile-Glu.

ISSN 

0916-8451

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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