2000年6月1日
Purification and biochemical properties of an N-hydroxyarylamine O-acetyltransferase from Escherichia coli
Biochimica et Biophysica Acta - General Subjects
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- 巻
- 1475
- 号
- 1
- 開始ページ
- 10
- 終了ページ
- 16
- 記述言語
- 英語
- 掲載種別
- DOI
- 10.1016/S0304-4165(00)00038-6
The N-hydroxyarylamine O-acetyltransferase of Escherichia coli has been expressed as a histidine tagged fusion protein and purified using immobilized nickel column chromatography. The molecular mass of the histidine tagged N-hydroxyarylamine O-acetyltransferase was estimated to be 60.0 kDa by gel filtration and 34.0 kDa by SDS-PAGE and DNA sequence, suggesting that the native enzyme exists as homo dimer. The catalytic properties were investigated using o-aminobenzoic acid as a substrate. No difference in acetyltransfer activity was observed between histidine tagged protein and untagged enzyme. Kinetic studies indicated a ping-pong bi bi mechanism of the catalysis. Inhibition by N-ethylmaleimide and salicylic acid was competitive with o-aminobenzoic acid and non-competitive with acetyl-CoA. Copyright (C) 2000 Elsevier Science B.V.
- リンク情報
- ID情報
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- DOI : 10.1016/S0304-4165(00)00038-6
- ISSN : 0304-4165
- PubMed ID : 10806332
- SCOPUS ID : 0034213759