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Arylamine N-acetyltransferase activity in Staphylococcus aureus
F C Chang1, J G Chung, W C Chang
1Department of Medicine, China Medical College, Taichung, Taiwan, Republic of China.
Zhonghua Minguo Wei Sheng Wu Ji Mian Yi Xue Za Zhi = Chinese Journal of Microbiology and Immunology
|August 1, 1997
Summary
This study demonstrates N-acetyltransferase (NAT) activity in Staphylococcus aureus, characterizing its kinetic properties and inhibition by iodoacetamide and divalent cations. This is the first report of arylamine NAT activity in S. aureus.
Area of Science:
- Biochemistry
- Microbiology
- Enzymology
Background:
- N-acetyltransferases (NATs) are crucial enzymes involved in xenobiotic metabolism.
- Staphylococcus aureus is a common human pathogen, and understanding its enzymatic machinery is vital for drug development.
Purpose of the Study:
- To characterize the N-acetyltransferase (NAT) activity in Staphylococcus aureus.
- To determine the kinetic parameters, optimal conditions, and inhibitors of S. aureus NAT.
- To report the first evidence of acetyl CoA: arylamine NAT activity in S. aureus.
Main Methods:
- Enzyme activity assays using p-aminobenzoic acid (PABA) and 2-aminofluorene (2-AF) as substrates.
- High-performance liquid chromatography (HPLC) for product quantification.
- Determination of kinetic parameters (Km, Vmax), optimal pH and temperature, and inhibitor profiles.
Main Results:
- S. aureus cytosol exhibited NAT activity with 2-AF (0.67 nmol/min/mg) and PABA (0.46 nmol/min/mg).
- Optimal activity was observed at pH 7.0 and 37°C for both substrates.
- Iodoacetamide and divalent cations (Zn2+, Ca2+, Fe2+) were potent inhibitors of NAT activity.
Conclusions:
- This study provides the first characterization of acetyl CoA: arylamine NAT activity in Staphylococcus aureus.
- The identified NAT enzyme has potential implications for understanding bacterial metabolism and developing novel antimicrobial strategies.