Results 141 to 150 of about 4,253 (187)

Quantitative Site-Specific Chemoproteomic Profiling of Protein Lipoylation

Journal of the American Chemical Society, 2022
Protein lipoylation is an evolutionarily conserved post-translational modification from prokaryotes to eukaryotes. Lipoylation is implicated with several human diseases, including metabolic disorders, cancer, and Alzheimer's disease. While individual lipoylated proteins have been biochemically studied, a strategy for globally quantifying lipoylation ...
Yuan Liu, Chu Wang, Weidi Xiao
exaly   +5 more sources

Solanum lycopersicum (tomato) possesses mitochondrial and plastidial lipoyl synthases capable of increasing lipoylation levels when expressed in bacteria [PDF]

Plant Physiology and Biochemistry, 2020
Lipoic acid (LA) and its reduced form (dihydrolipoic acid, DHLA) have unique antioxidant properties among such molecules. Moreover, after a process termed lipoylation, LA is an essential prosthetic group covalently-attached to several key multi-subunit enzymatic complexes involved in primary metabolism, including E2 subunits of pyruvate dehydrogenase ...
Claudia Stange, Michael Handford, Simon Miranda   +2 more
exaly   +5 more sources

A unique lipoylation system in the Archaea [PDF]

FEBS Journal, 2009
Members of the 2-oxoacid dehydrogenase multienzyme complex family play a key role in the pathways of central metabolism. Post-translational lipoylation of the dihydrolipoyl acyltransferase component of these complexes is essential for their activity, the lipoyllysine moiety performing the transfer of substrates and intermediates between the different ...
Mareike Posner, Stefan Bagby
exaly   +3 more sources

Mitochondrial lipoylation integrates age-associated decline in brown fat thermogenesis [PDF]

Nature Metabolism, 2019
Thermogenesis in brown adipose tissue (BAT) declines with age; however, what regulates this process is poorly understood. Here, we identify mitochondrial lipoylation as a previously unappreciated molecular hallmark of aged BAT in mice.
Takeshi Yoneshiro, Heejin Jun, Yasushi Ishihama   +2 more
exaly   +2 more sources

Activation and competition of lipoylation of H protein and its hydrolysis in a reaction cascade catalyzed by the multifunctional enzyme lipoate–protein ligase A

Biotechnology and Bioengineering, 2020
Protein lipoylation is essential for the function of many key enzymes but barely studied kinetically. Here, the two-step reaction cascade of H protein lipoylation catalyzed by the multifunctional enzyme lipoate–protein ligase A (LplA) was quantitatively ...
Jie Ren, An-Ping Zeng
exaly   +2 more sources

Functional Reconstitution of a Pyruvate Dehydrogenase in the Cytosol of Saccharomyces cerevisiae through Lipoylation Machinery Engineering

ACS Synthetic Biology, 2016
Acetyl-CoA is a key precursor for the biosynthesis of a wide range of fuels, chemicals, and value-added compounds, whose biosynthesis in Saccharomyces cerevisiae involves acetyl–CoA synthetase (ACS) and is energy intensive.
Jiazhang Lian, Huimin Zhao
exaly   +2 more sources

Some of the next articles are maybe not open access.

Related searches:

Chemical Tagging of Protein Lipoylation

Angewandte Chemie, 2020
AbstractProtein lipoylation is a post‐translational modification of emerging importance in both prokaryotes and eukaryotes. However, labeling and large‐scale profiling of protein lipoylation remain challenging. Here, we report the development of iLCL (iodoacetamide‐assisted lipoate‐cyclooctyne ligation), a chemoselective reaction that enables chemical ...
Qi Tang, Yilan Guo, Liying Meng, Xing Chen   +3 more
openaire   +2 more sources

N-lipoyl glucosamine and N-lipoyl glucosaminitol: Substrates for lipoyl dehydrogenase

Archives of Biochemistry and Biophysics, 1969
Abstract N - dl -Lipoyl- d -glucosamine and N - dl -lipoyl- d -glucosaminitol were prepared and tested as substrates for lipoyl dehydrogenase (reduced nicotinamide adenine dinucleotide: Lipoamide oxidoreductase, EC 1.6.4.3). It was anticipated that such lipoateamino carbohydrate derivatives would be superior substrates for the enzyme, having ...
A L, Fluharty, G L, Adelson, B P, Gaber
openaire   +2 more sources

Protein lipoylation: an evolutionarily conserved metabolic regulator of health and disease

Current Opinion in Chemical Biology, 2018
Lipoylation is a rare, but highly conserved lysine posttranslational modification. To date, it is known to occur on only four multimeric metabolic enzymes in mammals, yet these proteins are staples in the core metabolic landscape.
Ileana Cristea
exaly   +2 more sources