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- 鏡山 博行
- 大阪医科大学医化学
書誌事項
- タイトル別名
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- Recent Progress in Enzyme Chemistry of Aminotransferases
- ピリドキサール コウソ カガク ケンキュウ ノ ゲンジョウ アミノキ テンイ
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抄録
Pyridoxal enzymes catalyze versatile reactions with amino acids, including transamination, recemization, α, β-elimination, and decarboxylation. The reaction mechanism for these reactions has been explained on the basis of diverse chemical properties of pyridoxal phosphate. Recent progress in recombinant DNA techniques allowed us to examine the role of apoproteins of the pyridoxal enzymes at the atomic level based on crystallographic and sitedirected mutagenesis studies. Among the pyridoxal enzymes, aminotransferases, particularly aspartate aminotransferase, have been most extensively studied from structural and functional aspects. In this paper, I will describe some important information obtained recently on substrate recognition and transaldimination, which are the initial steps common to all the pyridoxal enzymes, centering discussion on the uniqueness of aspartate aminotransferase.
収録刊行物
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- ビタミン
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ビタミン 72 (3), 97-106, 1998
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
- 1390001205760742144
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- NII論文ID
- 110002843517
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- NII書誌ID
- AN00207833
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- ISSN
- 2424080X
- 0006386X
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- NDL書誌ID
- 4438328
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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
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- 抄録ライセンスフラグ
- 使用不可