Purification and Characterization of<i>N</i>-Acetylglucosamine 6-Phosphate Deacetylase with Activity against<i>N</i>-Acetylglucosamine from<i>Vibrio cholerae</i>Non-O1
書誌事項
- タイトル別名
-
- Purification and Characterization of N-Acetylglucosamine 6-Phosphate Deacetylase with Activity against N-Acetylglucosamine from Vibrio cholerae Non-O1.
- Purification and characterization of N-acetylglucosamine 6-phosphate deacetylase with activity against N-acetylglucosamine from Vibrio cholerae non-01
この論文をさがす
説明
An enzyme that doacetylates N-acetylglucosamine to glucosamine from Vibrio cholerae non-O1 was purified to homogeneity by sequential procedures. The native enzyme had a molecular mass of 190, 000 Da and was predicted to be composed of four identical subunits with molecular masses of 45, 000 Da. The purified enzyme hydrolyzed N-acetylglucosamine, N-acetylglucosamine 6-phosphate, and N-acetylglucosamine 6-sulfate, but not chitin oligosaccharides, and N-acetylgalactosamine. The deacetylase activity was completely abolished by N-ethylmaleimide, p-chloromercuribenzoate, EDTA, and Cu2+. On the other hand, the activity was activated by Co2+. The amino-terminal amino acids of the purified enzyme were sequenced. Among the 22 N-terminal amino acid residues, 12 residues of Vibrio deacetylase were identical with that of Escherichia coli GlcNAc 6-phosphate deacetylase.
収録刊行物
-
- Ｂｉｏｓｃｉｅｎｃｅ， Ｂｉｏｔｅｃｈｎｏｌｏｇｙ， ａｎｄ Ｂｉｏｃｈｅｍｉｓｔｒｙ
-
Ｂｉｏｓｃｉｅｎｃｅ， Ｂｉｏｔｅｃｈｎｏｌｏｇｙ， ａｎｄ Ｂｉｏｃｈｅｍｉｓｔｒｙ 60 (8), 1320-1323, 1996
公益社団法人 日本農芸化学会
- Tweet
詳細情報 詳細情報について
-
- CRID
- 1390282681453288320
-
- NII論文ID
- 110002678253
-
- NII書誌ID
- AA10824164
-
- ISSN
- 13476947
- 09168451
-
- PubMed
- 8987551
-
- 本文言語コード
- en
-
- 資料種別
- journal article
-
- データソース種別
-
- JaLC
- Crossref
- PubMed
- CiNii Articles
- OpenAIRE
-
- 抄録ライセンスフラグ
- 使用不可
