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

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Title
Purification and Characterization of the 2-ketoaldonate reductase from Brevibacterium ketosoreductum ATCC21914
Author(s)
Do Young Yum; Sung Sook Bae; Jae Gu Pan
Bibliographic Citation
Bioscience Biotechnology and Biochemistry, vol. 62, no. 1, pp. 154-156
Publication Year
1998
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.
Keyword
2-ketoaldonate reductaseBrevibacterium ketosoreductumketogluconate metabolism
ISSN
0916-8451
Publisher
T&F (Taylor & Francis)
DOI
http://dx.doi.org/10.1271/bbb.62.154
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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