PMID:10806332
| Citation |
Yamamura, E, Sayama, M, Kakikawa, M, Mori, M, Taketo, A and Kodaira, K (2000) Purification and biochemical properties of an N-hydroxyarylamine O-acetyltransferase from Escherichia coli. Biochim. Biophys. Acta 1475:10-6 |
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| Abstract |
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. |
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| Keywords |
Acetyl Coenzyme A/metabolism; Acetyltransferases; Acyltransferases/antagonists & inhibitors; Acyltransferases/isolation & purification; Acyltransferases/metabolism; Chromatography, Gel; Electrophoresis, Polyacrylamide Gel; Enzyme Inhibitors/pharmacology; Escherichia coli/enzymology; Kinetics; Plasmids; ortho-Aminobenzoates/metabolism |
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