Cutinase-like proteins of Mycobacterium tuberculosis: characterization of their variable enzymatic functions and active site identification

West, Nicholas P., Chow, Frances M. E., Randall, Elizabeth J., Wu, Jing, Chen, Jian, Ribeiro, Jose M. C. and Britton, Warwick J. (2009) Cutinase-like proteins of Mycobacterium tuberculosis: characterization of their variable enzymatic functions and active site identification. Faseb Journal, 23 6: 1694-1704. doi:10.1096/fj.08-114421


Author West, Nicholas P.
Chow, Frances M. E.
Randall, Elizabeth J.
Wu, Jing
Chen, Jian
Ribeiro, Jose M. C.
Britton, Warwick J.
Title Cutinase-like proteins of Mycobacterium tuberculosis: characterization of their variable enzymatic functions and active site identification
Journal name Faseb Journal   Check publisher's open access policy
ISSN 0892-6638
1530-6860
Publication date 2009-06
Year available 2009
Sub-type Article (original research)
DOI 10.1096/fj.08-114421
Open Access Status
Volume 23
Issue 6
Start page 1694
End page 1704
Total pages 11
Place of publication Bethesda, MD United States
Publisher Federation of American Societies for Experimental Biology
Collection year 2009
Language eng
Formatted abstract
 Discovery and characterization of novel secreted enzymes of Mycobacterium tuberculosis are important for understanding the pathogenesis of one of the most important human bacterial pathogens. The proteome of M. tuberculosis contains over 400 potentially secreted proteins, the majority of which are uncharacterized. A family of seven cutinase-like proteins (CULPs) was identified by bioinformatic analysis, expressed and purified from Escherichia coli, and characterized in terms of their enzymatic activities. These studies revealed a functional diversity of enzyme classes based on differential preferences for substrate chain length. One member, Culp1, exhibited strong esterase activity, 40-fold higher than that of Culp6, which had strong activity as a lipase. Another, Culp4, performed moderately as an esterase and weakly as a lipase. Culp6 lipase activity was optimal above pH 7.0, and fully maintained to pH 8.5. None of the CULP members exhibited cutinase activity. Site-directed mutagenesis of each residue of the putative catalytic triad in Culp6 confirmed that each was essential for activity toward all fatty acid chain lengths of nitrophenyl esters and lipolytic function. Culp1 and Culp2 were present only in culture supernatants of M. tuberculosis, while Culp6, which is putatively essential for mycobacterial growth, was retained in the cell wall, suggesting the proteins play distinct roles in mycobacterial biology.—West, N. P., Chow, F. M. E., Randall, E. J., Wu, J., Chen, J., Ribeiro, J. M. C., Britton, W. J. Cutinase-like proteins of Mycobacterium tuberculosis: characterization of their variable enzymatic functions and active site identification.
Keyword Secreted enzymes
Pathogenic Mycobacteria
Extracellular Lipase
Sequence Alignment
Lipolytic Enzymes
Culture Filtrate
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
 
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