Source:http://linkedlifedata.com/resource/pubmed/id/11932442
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
Pt 4
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| pubmed:dateCreated |
2002-4-4
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| pubmed:abstractText |
The fatty acid elongation system FAS-II is involved in the biosynthesis of mycolic acids, which are very long-chain fatty acids of the cell envelope specific to Mycobacterium tuberculosis and other mycobacteria. A potential component of FAS-II, the protein MabA (FabG1), was overexpressed and purified. Sedimentation equilibrium analyses revealed that MabA undergoes a dimer to tetramer self-association with a dissociation constant of 22 microM. The protein was detected by Western blotting in a mycobacterial cell-wall extract that produces mycolic acids and in the FPLC FAS-II fraction. MabA was shown to catalyse the NADPH-specific reduction of beta-ketoacyl derivatives, equivalent to the second step of a FAS-II elongation round. Unlike the known homologous proteins, MabA preferentially metabolizes long-chain substrates (C(8)-C(20)) and has a poor affinity for the C(4) substrate, in agreement with FAS-II specificities. Molecular modelling of MabA structure suggested the presence of an unusually hydrophobic substrate-binding pocket holding a unique Trp residue, suitable for fluorescence spectroscopic analyses. In agreement with the enzyme kinetic data, the spectral properties of MabA were different in the presence of the C(8)-C(16) ligands as compared to the C(4) ligand. Altogether, these data bring out distinctive enzymic and structural properties of MabA, which correlate with its predilection for long-chain substrates, in contrast to most of the other known ketoacyl reductases.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/3-oxoacyl-(acyl-carrier-protein)...,
http://linkedlifedata.com/resource/pubmed/chemical/Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Alcohol Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acid Synthetase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acid Synthetase Complex...,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids, Nonesterified,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Mycolic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/fatty acid synthase I, mycobacteria
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| pubmed:status |
MEDLINE
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| pubmed:month |
Apr
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| pubmed:issn |
1350-0872
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
148
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
951-60
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| pubmed:dateRevised |
2007-11-15
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| pubmed:meshHeading |
pubmed-meshheading:11932442-Acetyltransferases,
pubmed-meshheading:11932442-Alcohol Oxidoreductases,
pubmed-meshheading:11932442-Amino Acid Sequence,
pubmed-meshheading:11932442-Bacterial Proteins,
pubmed-meshheading:11932442-DNA Primers,
pubmed-meshheading:11932442-Fatty Acid Synthetase Complex,
pubmed-meshheading:11932442-Fatty Acid Synthetase Complex, Type II,
pubmed-meshheading:11932442-Fatty Acids, Nonesterified,
pubmed-meshheading:11932442-Kinetics,
pubmed-meshheading:11932442-Models, Molecular,
pubmed-meshheading:11932442-Molecular Sequence Data,
pubmed-meshheading:11932442-Multienzyme Complexes,
pubmed-meshheading:11932442-Mycobacterium tuberculosis,
pubmed-meshheading:11932442-Mycolic Acids,
pubmed-meshheading:11932442-Protein Conformation,
pubmed-meshheading:11932442-Sequence Alignment,
pubmed-meshheading:11932442-Sequence Homology, Amino Acid,
pubmed-meshheading:11932442-Substrate Specificity
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| pubmed:year |
2002
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| pubmed:articleTitle |
MabA (FabG1), a Mycobacterium tuberculosis protein involved in the long-chain fatty acid elongation system FAS-II.
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| pubmed:affiliation |
Institut de Pharmacologie et de Biologie Structurale, Centre National de la Recherche Scientifique, Université Paul Sabatier (UMR5089), 205 route de Narbonne, 31077 Toulouse cedex, France.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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