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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2007-11-23
pubmed:abstractText
The Rv0183 gene of the Mycobacterium tuberculosis H37Rv strain, which has been implicated as a lysophospholipase, was cloned and expressed in Escherichia coli. The purified Rv0183 protein did not show any activity when lysophospholipid substrates were used, but preferentially hydrolysed monoacylglycerol substrates with a specific activity of 290 units x mg(-1) at 37 degrees C. Rv0183 hydrolyses both long chain di- and triacylglycerols, as determined using the monomolecular film technique, although the turnover was lower than with MAG (monoacyl-glycerol). The enzyme shows an optimum activity at pH values ranging from 7.5 to 9.0 using mono-olein as substrate and is inactivated by serine esterase inhibitors such as E600, PMSF and tetrahydrolipstatin. The catalytic triad is composed of Ser110, Asp226 and His256 residues, as confirmed by the results of site-directed mutagenesis. Rv0183 shows 35% sequence identity with the human and mouse monoglyceride lipases and well below 15% with the other bacterial lipases characterized so far. Homologues of Rv0183 can be identified in other mycobacterial genomes such as Mycobacterium bovis, Mycobacterium smegmatis, and even Mycobacterium leprae, which is known to contain a low number of genes involved in the replication process within the host cells. The results of immunolocalization studies performed with polyclonal antibodies raised against the purified recombinant Rv0183 suggested that the enzyme was present only in the cell wall and culture medium of M. tuberculosis. Our results identify Rv0183 as the first exported lipolytic enzyme to be characterized in M. tuberculosis and suggest that Rv0183 may be involved in the degradation of the host cell lipids.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-10510226, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-10733881, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-11208107, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-11211933, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-11271494, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-11470505, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-11491291, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-11728873, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-12031661, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-12100560, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-12368428, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-12368430, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-12410824, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-12466875, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-12657046, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-13366889, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-13403178, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-13650640, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-14569030, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-15260473, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-15262939, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-15373841, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-15550674, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-15716583, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-15901682, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-15939293, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-16091048, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-16354661, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-16675698, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-17183672, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-17269661, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-18200, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-4208670, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-4594739, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-4698875, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-4970646, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-5154882, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-5321489, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-7149237, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-7950403, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-8526865, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-8610181, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-889853, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-9328647, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-9341166, http://linkedlifedata.com/resource/pubmed/commentcorrection/17784850-9634230
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1470-8728
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
408
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
417-27
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Characterization of an exported monoglyceride lipase from Mycobacterium tuberculosis possibly involved in the metabolism of host cell membrane lipids.
pubmed:affiliation
Laboratoire d'Enzymologie Interfaciale et de Physiologie de la Lipolyse, UPR 9025 - CNRS, 31 Chemin Joseph Aiguier, F-13402 Marseille Cedex 20, France.
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