Role of Conserved Histidine Residues in<scp>D</scp>-Aminoacylase from<i>Alcaligenes xylosoxydans</i>subsp.<i>xylosoxydans</i>A-6
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- WAKAYAMA Mamoru
- Department of Applied Chemistry, Faculty of Engineering
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- YADA Harutaka
- Department of Applied Chemistry, Faculty of Engineering
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- KANDA Shun-ichi
- Department of Applied Chemistry, Faculty of Engineering
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- HAYASHI Shin-ichi
- Department of Applied Chemistry, Faculty of Engineering
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- YATSUDA Yukinori
- Department of Applied Chemistry, Faculty of Engineering
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- SAKAI Kenji
- Department of Applied Chemistry, Faculty of Engineering
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- MORIGUCHI Mitsuaki
- Department of Applied Chemistry, Faculty of Engineering
書誌事項
- タイトル別名
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- Role of Conserved Histidine Residues in D-Aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6.
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抄録
D-Aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6 (Alcaligenes A-6) was strongly inactivated by diethylpyrocarbonate (DEPC). An H67N mutant was barely active, with a kcat/Km 6.3×104 times lower than that of the recombinant wild-type enzyme, while the H67I mutant lost detectable activity. The H67N mutant had almost constant Km, but greatly decreased kcat. These results suggested that His67 is essential to the catalytic event. Both H69N and H69I mutants were overproduced in the insoluble fraction. The kcat/Km of H250N mutant was reduced by a factor of 2.5×104-fold as compared with the wild-type enzyme. No significant difference between H251N mutant and wild-type enzymes in the Km and kcat was found. The Zn content of H250N mutant was nearly half of that of wild-type enzyme. These results suggest that the His250 residue might be essential to catalysis via Zn binding.<br>
収録刊行物
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 64 (1), 1-8, 2000
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
- 1390282681450751616
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- NII論文ID
- 110002679739
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- NII書誌ID
- AA10824164
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- DOI
- 10.1271/bbb.64.1
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- COI
- 1:CAS:528:DC%2BD3cXhtVyitL0%3D
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- ISSN
- 13476947
- 09168451
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- NDL書誌ID
- 5142906
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- PubMed
- 10705441
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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