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Showing 1 to 11 of 11 for “"lipoate"”.
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Lipoate-protein and biotin-protein ligases of Escherichia coli
Lipoate and biotin are critical and almost universally distributed cofactors which share striking parallels. Both cofactors are covalently attached to specific lysine residues of specific apoprotein domains, and thus function as protein bound carriers of reaction intermediates between separate …
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Studies of lipoic acid and biotin metabolism in bacteria and higher eukaryotes
… assays. In the second chapter I investigated the lipoate-protein liagase (LplA) from Streptomyces coelicolor. LplA enzymes function to scavenge lipoic acid from the environment and attach the coenzyme to its cognate proteins, which are generally the E2 components of the 2-oxoacid dehydrogenases. …
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Oral epithelium in the pathogenesis of periodontitis
… using a natural di-thiol antioxidant \(\alpha\)-lipoate was also investigated. Data demonstrated that periodontal pathogens P. gingivalis and F. nucleatum elicited a pro-inflammatory response in the H400 model system. This was confirmed by demonstrating NF-\(\kappa\)B activation, gene expression …
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Enzymatic diversity in lipoic acid modification of proteins
… examining the distribution and phylogeny of the lipoate ligase protein family, I and others have found gaps and inconsistencies in our knowledge of lipoic acid metabolic pathways. I examine select proteins through heterologous expression in E. coli, allowing complementation studies and …
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Studies on lipoic acid metabolism
… octanoate can be directly attached to the LDs by lipoate-protein ligase (LplA) via an acyl–AMP intermediate. E. coli strains containing null mutations in lipB are auxotrophic for either lipoic acid (or octanoate), or acetate plus succinate which respectively bypass the PDH- and OGDH-catalyzed …
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Post-Translational Modification With Lipoic Acid in Escherichia Coli
… The first pathway identified involves the lplA (lipoate-protein ligase) gene product, which utilizes free lipoic acid found in the environment to modify apoproteins. A second pathway was known to be dependent on lipB. I have identified lipB as the structural gene involved in the second, lplA …
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Lipoic acid assembly on 2-oxoacid dehydrogenases in E.coli
… components are present. In contrast LplA, the lipoate protein ligase enzyme of lipoate salvage, shows no interaction with the 2-oxoacid dehydrogenases. The interaction is specific to the dehydrogenases in that the third lipoic acid requiring enzyme of E. coli, the glycine cleavage system H …
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Crystallization studies of 5'-deoxyadenosyl radical enzymes
… without cobalamin to try to solve its structure. Lipoate synthase is another Sadenosylmethionine-dependent radical enzyme, performing two sulfur insertion reactions on a protein-bound octanoyl group to form a lipoyl group. Crystallization experiments were performed on this enzyme, with and without …
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Lipoic acid protein ligases in Plasmodium spp.
… in an ATP-dependent reaction. However, a second lipoate protein ligase A (LplA2) was identified in the genome of P. falciparum, but its subcellular localisation could not be predicted using the available prediction programs. To further analyse its localisation, parasites were generated expressing …
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Lipoic acid metabolism in Leishmania major
… protein N-octanoyltransferase (LIPB) and lipoate protein ligase (LPLA), respectively), and it was predicted that all three proteins possess mitochondrial targeting peptides. Targeting of these proteins to the mitochondrion was verified by a green fluorescence protein (GFP) reporter system, …
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The role of ABHD11 in the regulation of the hypoxia inducible transcription factors
Hypoxia inducible transcription factors (HIFs) mediate a highly conserved cellular oxygen sensing system, driving a diverse set of transcriptional changes that allow adaptation to hypoxic conditions. However, HIFs can also be activated independently of oxygen by changes in levels of mitochondrial …