書誌事項
- タイトル別名
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- Structure and function of alginate-metabolizing enzymes
- アルギンサン タイシャ コウソ ノ コウゾウ ト キノウ
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抄録
A gram-negative and alginate-assimilating bacterium, Sphingomonas sp. A1, can incorporate the polysaccharide into the cytoplasm through the cell-surface pit and ABC transporter. Alginate is depolymerized into disaccharides to tetrasaccharides by cytoplasmic endotype alginate lyases (A1-I, II, III). An exotype alginate lyase A1-IV degrades the oligosaccharides to unsaturated monosaccharides. α-Keto acids nonenzymatically formed from monosaccharides are converted to 2-keto-3-deoxy-^D-gluconic acid (KDG) by NADPH-dependent reductase A1-R. KDG is eventually metabolized to glyceraldehyde-3-phosphate and pyruvate through the sequential reaction catalyzed by KDG kinase (A1-K) and 2-keto-3-deoxy 6-phosphogluconate aldolase (A1-A). This review deals with the structure and function of bacterial alginate-metabolizing enzymes, especially structure determinants responsible for the catalytic reaction and mode of action of endotype lyases A1-II, II', III in strain A1 and exotype lyase Atu3025 in Agrobacterium tumefaciens as well as for the coenzyme-binding mode of strain A1 α-keto acid reductase (A1-R).
収録刊行物
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- ビタミン
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ビタミン 84 (11), 525-531, 2010
公益社団法人 日本ビタミン学会
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詳細情報 詳細情報について
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- CRID
- 1390001205700857344
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- NII論文ID
- 110007989343
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- NII書誌ID
- AN00207833
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- ISSN
- 2424080X
- 0006386X
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- NDL書誌ID
- 10913456
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- NDL
- CiNii Articles
- KAKEN
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- 抄録ライセンスフラグ
- 使用不可