Overexpression and Mechanistic Analysis of Chromosomally Encoded Aminoglycoside 2′-N-Acetyltransferase (AAC(2′)-Ic) fromMycobacterium tuberculosis
The chromosomally encoded aminoglycosideN-acetyltransferase, AAC(2′)-Ic, of Mycobacterium tuberculosis has a yet unidentified physiological function. Theaac(2′)-Ic gene was cloned and expressed inEscherichia coli, and AAC(2′)-Ic was purified. Recombinant AAC(2′)-Ic was a soluble protein of 20,000 Da...
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Published in | The Journal of biological chemistry Vol. 276; no. 49; pp. 45876 - 45881 |
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Format | Journal Article |
Language | English |
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07.12.2001
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Abstract | The chromosomally encoded aminoglycosideN-acetyltransferase, AAC(2′)-Ic, of Mycobacterium tuberculosis has a yet unidentified physiological function. Theaac(2′)-Ic gene was cloned and expressed inEscherichia coli, and AAC(2′)-Ic was purified. Recombinant AAC(2′)-Ic was a soluble protein of 20,000 Da and acetylated all aminoglycosides substrates tested in vitro, including therapeutically important antibiotics. Acetyl-CoA was the preferred acyl donor. The enzyme, in addition to acetylating aminoglycosides containing 2′-amino substituents, also acetylated kanamycin A and amikacin that contain a 2′-hydroxyl substituent, although with lower activity, indicating the capacity of the enzyme to perform bothN-acetyl and O-acetyl transfer. The enzyme exhibited “substrate activation” with many aminoglycoside substrates while exhibiting Michaelis-Menten kinetics with others. Kinetic studies supported a random kinetic mechanism for AAC(2′)-Ic. Comparison of the kinetic parameters of different aminoglycosides suggested that their hexopyranosyl residues and, to a lesser extent, the central aminocyclitol residue carry the major determinants of substrate affinity. |
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AbstractList | The chromosomally encoded aminoglycosideN-acetyltransferase, AAC(2′)-Ic, of Mycobacterium tuberculosis has a yet unidentified physiological function. Theaac(2′)-Ic gene was cloned and expressed inEscherichia coli, and AAC(2′)-Ic was purified. Recombinant AAC(2′)-Ic was a soluble protein of 20,000 Da and acetylated all aminoglycosides substrates tested in vitro, including therapeutically important antibiotics. Acetyl-CoA was the preferred acyl donor. The enzyme, in addition to acetylating aminoglycosides containing 2′-amino substituents, also acetylated kanamycin A and amikacin that contain a 2′-hydroxyl substituent, although with lower activity, indicating the capacity of the enzyme to perform bothN-acetyl and O-acetyl transfer. The enzyme exhibited “substrate activation” with many aminoglycoside substrates while exhibiting Michaelis-Menten kinetics with others. Kinetic studies supported a random kinetic mechanism for AAC(2′)-Ic. Comparison of the kinetic parameters of different aminoglycosides suggested that their hexopyranosyl residues and, to a lesser extent, the central aminocyclitol residue carry the major determinants of substrate affinity. |
Author | Blanchard, John S. Javid-Majd, Farah Hegde, Subray S. |
Author_xml | – sequence: 1 givenname: Subray S. surname: Hegde fullname: Hegde, Subray S. – sequence: 2 givenname: Farah surname: Javid-Majd fullname: Javid-Majd, Farah – sequence: 3 givenname: John S. surname: Blanchard fullname: Blanchard, John S. email: blanchar@aecom.yu.edu |
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