書誌事項
- タイトル別名
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- Development of the Regio- and Stereospecific Proline Hydroxylases and Their Application.
- イチ オヨビ リッタイ センタクテキ プロリン スイサンカ コウソ ノ カイハツ ト ソノ オウヨウ
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This article describes microbial proline hydroxylases which carry out regio- and stereospecific hydroxylation of free L-proline and their application to the enzymatic synthesis of hydroxyprolines and related compounds. Proline 4-hydroxylase activities were detected in 8 actinomycetes strains, and proline 3-hydroxylase activities were detected in 3 actinomycetes and 2 Bacillus strains. Both enzymes were purified and characterized. The enzymes required 2-oxoglutarate and Fe2+ for the reaction. Proline 4-hydroxylase hydroxylated L-proline in a regio- and stereospecific manner at C-4 to form trans-4-hydroxy-L-proline, while 3-hydroxylase hydroxylated C-3 of L-proline to form cis-3-hydroxy-L-proline. Efficient biotransformation systems of L-proline to trans-4-hydroxy-L-proline or cis-3-hydroxy-L-proline were established using recombinant DNA technology. Both of the enzymes hydroxylated L-2-azetidine carboxylate, 3, 4-dehydro-L-proline and L-pipecolate in a regio- and stereospecific manner, however, D-proline, N-substituted L-proline, L-proline ester and peptidyl L-proline do not react as substrates for either 4- or 3-hydroxylases.
収録刊行物
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- 有機合成化学協会誌
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有機合成化学協会誌 57 (6), 523-531, 1999
公益社団法人 有機合成化学協会
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詳細情報 詳細情報について
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- CRID
- 1390001205279036544
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- NII論文ID
- 10009348066
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- NII書誌ID
- AN0024521X
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- ISSN
- 18836526
- 00379980
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- NDL書誌ID
- 4756286
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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
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- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可