Kinetics of inactivation of WT and C243S mutant of Mycobacterium tuberculosis enoyl reductase by activated isoniazid

Journal of the American Chemical Society

Volumn 118, Issue 45, 1996, Pages 11301-11302

  Basso, Luiz A ^a   Zheng, Renjian ^a   Blanchard, John S ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ISONIAZID; OXIDOREDUCTASE;

ARTICLE; DRUG ACTIVATION; ENZYME ACTIVITY; ENZYME INHIBITION; MUTANT; MYCOBACTERIUM TUBERCULOSIS;

EID: 0029860774     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja962035y     Document Type: Article

References (19)

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13. 13 was used to screen the colonies harboring the mutated gene. Liquid chromatography-electrospray mass spectrometry (LC/MS) was performed on both wild-type and C243S enzymes, which were purified according to the protocol described elsewhere,' in order to confirm that no unexpected mutations were introduced and the identity of the mutated enzyme. The deconvoluted data for the subunit molecular mass yielded values of 28 371 and 28 355 Da for wild-type and mutant enzymes, respectively, confirming the substitution of a sulfur for an oxygen atom.
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15. -1, respectively.
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