Linked Life Data

20103719

Source:http://linkedlifedata.com/resource/pubmed/id/20103719

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2010-6-2
pubmed:abstractText
Cutinases are extracellular enzymes that are able to degrade cutin, a polyester protecting plant leaves and many kinds of lipids. Although cutinases are mainly found in phytopathogenic fungi or bacteria, 7 genes related to the cutinase family have been predicted in the genome of Mycobacterium tuberculosis. These genes may encode proteins that are involved in the complex lipid metabolism of the bacterium. Here, we report on the biochemical characterization of two secreted proteins of M. tuberculosis, Rv1984c and Rv3452, belonging to the cutinase family. Although their amino acid sequence shows 50% identity with that of the well-characterized cutinase from Fusarium solani pisi, and a high level of homology has been found to exist between these two enzymes, they show distinct substrate specificities. Rv1984c preferentially hydrolyzes medium-chain carboxylic esters and monoacylglycerols, whereas Rv3452 behaves like a phospholipase A(2), and it is able to induce macrophage lysis. The tetrahydrolipstatin inhibitor, a specific lipase inhibitor, abolishes the activity of both enzymes. Site-directed mutagenesis was performed to identify the catalytic triad of Rv1984c. Structural models for Rv1984c and Rv3452 were built, based on the crystal structure of F. solani cutinase, with a view to investigating the contribution of specific residues to the substrate specificity. Our findings open new prospects for investigating the physiological roles of cutinase-like proteins in the lipid metabolism and virulence of M. tuberculosis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1530-6860
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1893-903
pubmed:dateRevised
2010-10-1
pubmed:meshHeading
pubmed-meshheading:20103719-Amino Acid Sequence, pubmed-meshheading:20103719-Animals, pubmed-meshheading:20103719-Carboxylic Ester Hydrolases, pubmed-meshheading:20103719-Catalysis, pubmed-meshheading:20103719-Enzyme Inhibitors, pubmed-meshheading:20103719-Esters, pubmed-meshheading:20103719-Lactones, pubmed-meshheading:20103719-Lipase, pubmed-meshheading:20103719-Lipolysis, pubmed-meshheading:20103719-Macrophages, pubmed-meshheading:20103719-Mice, pubmed-meshheading:20103719-Molecular Sequence Data, pubmed-meshheading:20103719-Mutagenesis, Site-Directed, pubmed-meshheading:20103719-Mycobacterium tuberculosis, pubmed-meshheading:20103719-Phospholipases A2, pubmed-meshheading:20103719-Protein Conformation, pubmed-meshheading:20103719-Sequence Homology, Amino Acid, pubmed-meshheading:20103719-Substrate Specificity
pubmed:year
2010
pubmed:articleTitle
Two cutinase-like proteins secreted by Mycobacterium tuberculosis show very different lipolytic activities reflecting their physiological function.
pubmed:affiliation
Centre National de la Recherche Scientifique, Aix-Marseille Université, Enzymologie Interfaciale et Physiologie de la Lipolyse UPR 9025, Marseille, France.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't