ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2009
Cutinase-like proteins of Mycobacterium tuberculosis: characterization of their variable enzymatic functions and active site identification.
Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 68 citations in OpenAlex.
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- Integrated sequence and -omic features reveal novel small proteome ofFrontiers in microbiology · 2024Article
- Roles of Lipolytic enzymes inFrontiers in microbiology · 2024Review
- Identification of cell wall synthesis inhibitors active against Mycobacterium tuberculosis by competitive activity-based protein profiling.Cell chemical biology · 2022Article
- A Novel Actinobacterial Cutinase Containing a Noncatalytic Polymer-Binding Domain.Applied and environmental microbiology · 2022Article
- Phylogenetic analysis and in-depth characterization of functionally and structurally diverse CE5 cutinases.The Journal of biological chemistry · 2021Article
- Exploring the Enzymatic and Antibacterial Activities of Novel Mycobacteriophage Lysin B Enzymes.International journal of molecular sciences · 2020Article
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- Biochemical and microbiological evaluation ofMedChemComm · 2019Article
- LipG a bifunctional phospholipase/thioesterase involved in mycobacterial envelope remodeling.Bioscience reports · 2018Article
- Delineating the Physiological Roles of the PE and Catalytic Domains of LipY in Lipid Consumption in Mycobacterium-Infected Foamy Macrophages.Infection and immunity · 2018Article
- Characterization of Tetrahydrolipstatin and Stereoderivatives on the Inhibition of Essential Mycobacterium tuberculosis Lipid Esterases.Biochemistry · 2018Article
- Structural basis for lipid binding and mechanism of theThe Journal of biological chemistry · 2018Article
- B cells response directed against Cut4 and CFP21 lipolytic enzymes in active and latent tuberculosis infections.PloS one · 2018Article
- Downstream process development strategies for effective bioprocesses: Trends, progress, and combinatorial approaches.Engineering in life sciences · 2017Article
- Ester-prodrugs of ethambutol control its antibacterial activity and provide rapid screening for mycobacterial hydrolase activity.Bioorganic & medicinal chemistry letters · 2017Article
- Identification of Mycobacterium avium subsp. hominissuis secreted proteins using an in vitro system mimicking the phagosomal environment.BMC microbiology · 2016Article
- Bacterial Sphingomyelinases and Phospholipases as Virulence Factors.Microbiology and molecular biology reviews : MMBR · 2016Review
- Profiling Esterases in Mycobacterium tuberculosis Using Far-Red Fluorogenic Substrates.ACS chemical biology · 2016Article
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Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
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.
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