Recombinant<i>Agrobacterium</i>AgaE-like Protein with Fructosyl Amino Acid Oxidase Activity
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- HIROKAWA Kozo
- <i>Research and Development Division, Kikkoman Corporation</i>
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- KAJIYAMA Naoki
- <i>Research and Development Division, Kikkoman Corporation</i>
書誌事項
- タイトル別名
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- Recombinant Agrobacterium AgaE-like Protein with Fructosyl Amino Acid Oxidase Activity.
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説明
Agrobacterium tumefaciens AgaE-like protein had a similar sequence to that of a fructosyl amino acid oxidase from Corynebacterium sp. strain 2-4-1. To characterize the AgaE-like protein, we produced the enzyme in Escherichia coli, and purified it to homogeneity. The molecular mass of recombinant AgaE-like protein was 42 kDa on SDS-PAGE and 85 kDa on gel filtration. The protein acted on N-fructosyl valine and N-fructosyl glycine as substrates, but not on glycated protein or Nε-fructosyl lysine. Apparent Km for N-fructosyl valine and N-fructosyl glycine were 1.64 and 0.31 mM, respectively. The AgaE-like protein had maximum activity at pH 7.8 and 35°C in 0.1 M potassium phosphate, but more than 80% of its activity was lost at 40°C or more. In contrast to eukaryotic fructosyl amino acid oxidases, the AgaE-like protein contained noncovalently bound FAD as a cofactor and was inactive against Nε-fructosyl Nα-Z(benzyloxycarbonyl)-lysine. These characteristics were similar to a fructosyl amino acid oxidase from Corynebacterium sp. strain 2-4-1, suggesting that these prokaryotic enzymes comprise a new family of fructosyl amino acid oxidases.<br>
収録刊行物
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 66 (11), 2323-2329, 2002
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390001206474131072
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- NII論文ID
- 110002693560
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- NII書誌ID
- AA10824164
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- COI
- 1:CAS:528:DC%2BD38XpsVOisb4%3D
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- ISSN
- 13476947
- 09168451
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- NDL書誌ID
- 6362530
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- PubMed
- 12506967
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可