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Showing 1 to 12 of 12 for “"LplA"”.
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Rational design and directed evolution of probe ligases for site-specific protein labeling and live-cell imaging
… the E. coli enzyme, lipoic acid ligase (LplA), to catalyze the ligation of small-molecule probes onto recombinant proteins. We call this collection of methods the PRIME (PRobe Incorporation Mediated by Enzymes) methodologies. First, we describe the structure-guided mutagenesis of LplA and …
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Log-Periodic Loop Antennas
… Log-Periodic Loop Antenna with Ground Reflector (LPLA-GR) is investigated as a new type of antenna, which provides wide bandwidth, broad beamwidth, and high gain. This antenna has smaller transverse dimensions (by a factor of 2/pi) than a log-periodic dipole antenna with comparable radiation …
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Lipoic acid metabolism in Leishmania major
… (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, and by subcellular …
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Studies on lipoic acid metabolism
… 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 steps required for aerobic …
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Extending the utility of enzymes for site-specific targeting of fluorescent probes
… be directly bound by the enzyme we engineered LplA to incorporate functional handles that can be chemoselectively derivatized with fluorophores in a second step. In one example, LplA targeted a strained alkene to cellular proteins, which can subsequently react with dienophiles with exceptional …
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Studies of lipoic acid and biotin metabolism in bacteria and higher eukaryotes
… 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. The LplA reaction is …
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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, …
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Chemical and enzymatic tools to study proteins in their native cellular environment
… methodology uses the E. coli lipoic acid ligase (LplA) that we have engineered to accept and ligate an azide functional handle onto a 13-amino acid ḺplA a̲cceptor peptide (LAP). Subsequent derivatization of the azide with fluorophores functionalized with cyclooctyne via strain-promoted …
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Cellular delivery and site-specific targeting of organic fluorophores for super-resolution imaging in living cells
… specificity for E. coli lipoic acid ligase (LplA), we created a mutant ligase that catalyzes covalent conjugation of a 7-hydroxycoumarin fluorophore onto a 13-amino acid peptide substrate, called LAP. We showed that enzymatic fluorophore ligation is compatible with the living cell interior …
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Lipoic acid assembly on 2-oxoacid dehydrogenases in E.coli
… lipoic acid scavenging pathway catalyzed by the LplA protein. LipB is responsible for octanoylation of the E2 components of 2-oxoacid dehydrogenases to provide the substrates of LipA, a SAM radical enzyme that inserts two sulfur atoms into the octanoyl moiety to give the active lipoylated …
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Lipoic acid protein ligases in Plasmodium spp.
… by the action of lipoic acid protein ligase A (LplA1), 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 …
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Immunological and biosynthetic studies of the human pyruvate dehydrogenase complex
… agents serving as substrates for E. coli LplA ligase, the non-lipoylated domain of human ILD-PDC (produced in the absence of the exogenous lipoic acid) was modified in vitro with various lengths of saturated fatty acids (C2-C14) and related compounds. These included a branched-chain fatty …