Molecular Basis of the Functional Divergence of Fatty Acyl-AMP Ligase Biosynthetic Enzymes of Mycobacterium tuberculosis
Journal of Molecular Biology, ISSN: 0022-2836, Vol: 416, Issue: 2, Page: 221-238
2012
- 40Citations
- 87Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations40
- Citation Indexes40
- 40
- CrossRef27
- Captures87
- Readers87
- 87
Article Description
Activation of fatty acids as acyl-adenylates by fatty acyl-AMP ligases (FAALs) in Mycobacterium tuberculosis is a variant of a classical theme that involves formation of acyl-CoA (coenzyme A) by fatty acyl-CoA ligases (FACLs). Here, we show that FAALs and FACLs possess similar structural fold and substrate specificity determinants, and the key difference is the absence of a unique insertion sequence in FACL13 structure. A systematic analysis shows a conserved hydrophobic anchorage of the insertion motif across several FAALs. Strikingly, mutagenesis of two phenylalanine residues, which are part of the anchorage, to alanine converts FAAL32 to FACL32. This insertion-based in silico analysis suggests the presence of FAAL homologues in several other non-mycobacterial genomes including eukaryotes. The work presented here establishes an elegant mechanism wherein an insertion sequence drives the functional divergence of FAALs from canonical FACLs.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0022283611013350; http://dx.doi.org/10.1016/j.jmb.2011.12.031; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84856437600&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/22206988; https://linkinghub.elsevier.com/retrieve/pii/S0022283611013350; https://dx.doi.org/10.1016/j.jmb.2011.12.031
Elsevier BV
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