Purification and biochemical properties of an N-hydroxyarylamine O-acetyltransferase from Escherichia coli

• Published in: Biochimica et biophysica acta Vol. 1475; no. 1; pp. 10 - 16
• Main Authors: Yamamura, Ei-Tora, Sayama, Michio, Kakikawa, Makiko, Mori, Masa-aki, Taketo, Akira, Kodaira, Ken-Ichi
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.06.2000
• Subjects: Acetyl Coenzyme A - metabolism; Acetyl-CoA; Acetyltransferases; Acyltransferases - antagonists & inhibitors; Acyltransferases - isolation & purification; Acyltransferases - metabolism; Chromatography, Gel; Dimer; Electrophoresis, Polyacrylamide Gel; Enzyme Inhibitors - pharmacology; Escherichia coli - enzymology; Histidine tag; Kinetics; N-hydroxyarylamine O-acetyltransferase; o-Aminobenzoic acid; ortho-Aminobenzoates - metabolism; Ping-pong bi bi; Plasmids; Ping-pong bi bi; N-hydroxyarylamine O-acetyltransferase; Histidine tag; Dimer; Acetyl-CoA; o-Aminobenzoic acid

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 fi...