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Temperature stability of proteins essential for the intracellular survival of Mycobacterium tuberculosis
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Lack, Nathan A, Kawamura, Akane, Fullam, Elizabeth, Laurieri, Nicola, Beard, Stacey, Russell, Angela J, Evangelopoulos, Dimitrios, Westwood, Isaac and Sim, Edith (2008) Temperature stability of proteins essential for the intracellular survival of Mycobacterium tuberculosis. The Biochemical journal, Volume 418 (Number 2). pp. 369-78. doi:10.1042/BJ20082011 ISSN 1470-8728.
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Official URL: http://dx.doi.org/10.1042/BJ20082011
Abstract
In Mycobacterium tuberculosis, the genes hsaD (2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid hydrolase) and nat (arylamine N-acetyltransferase) are essential for survival inside of host macrophages. These genes act as an operon and have been suggested to be involved in cholesterol metabolism. However, the role of NAT in this catabolic pathway has not been determined. In an effort to better understand the function of these proteins, we have expressed, purified and characterized TBNAT (NAT from M. tuberculosis) and HsaD (2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid hydrolase) from M. tuberculosis. Both proteins demonstrated remarkable heat stability with TBNAT and HsaD retaining >95% of their activity after incubation at 60 degrees C for 30 min. The first and second domains of TBNAT were demonstrated to be very important to the heat stability of the protein, as the transfer of these domains caused a dramatic reduction in the heat stability. The specific activity of TBNAT was tested against a broad range of acyl-CoA cofactors using hydralazine as a substrate. TBNAT was found to be able to utilize not just acetyl-CoA, but also n-propionyl-CoA and acetoacetyl-CoA, although at a lower rate. As propionyl-CoA is a product of cholesterol catabolism, we propose that NAT could have a role in the utilization of this important cofactor.
Item Type: | Journal Article | ||||
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||
Journal or Publication Title: | The Biochemical journal | ||||
Publisher: | Portland Press | ||||
ISSN: | 1470-8728 | ||||
Official Date: | 18 November 2008 | ||||
Dates: |
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Volume: | Volume 418 | ||||
Number: | Number 2 | ||||
Page Range: | pp. 369-78 | ||||
DOI: | 10.1042/BJ20082011 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Restricted or Subscription Access |
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