Results 151 to 160 of about 3,788 (176)

Lipoylation of H-protein of the glycine cleavage system The effect of site-directed mutagenesis of amino acid residues around the lipoyllysine residue on the lipoate attachment

FEBS Letters, 1991
H-protein of the glycine cleavage system has lipoic acid on the Lys59 residue. Comparison of amino acid sequences around the lipoate attachment site of H-proteins from various sources and acyltransferases of α-keto acid dehydrogenase complexes indicated ...
Kazuko Fujiwara, Kazuko Okamura-Ikeda, Yutaro Motokawa   +2 more
exaly   +2 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 G Posner, Abhishek Upadhyay, Stefan Bagby   +2 more
exaly   +3 more sources

Engineered bacterial lipoate protein ligase A (lplA) restores lipoylation in cell models of lipoylation deficiency

Journal of Biological Chemistry
Protein lipoylation, a vital lysine post-translational modification, plays a crucial role in the function of key mitochondrial tricarboxylic acid cycle enzymatic complexes. In eukaryotes, lipoyl post-translational modification synthesis occurs exclusively through de novo pathways, relying on lipoyl synthesis/transfer enzymes, dependent upon ...
Mark D Fleming, Peter Tsvetkov, Nolan R Bick   +2 more
exaly   +3 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

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Copper induces cell death by targeting lipoylated TCA cycle proteins

Science, 2022
Copper is an essential cofactor for all organisms, and yet it becomes toxic if concentrations exceed a threshold maintained by evolutionarily conserved homeostatic mechanisms. How excess copper induces cell death, however, is unknown. Here, we show in human cells that copper-dependent, regulated cell death is distinct from known death mechanisms and is
Peter Tsvetkov, Shannon Coy, Boryana Petrova, Margaret Dreishpoon, Ana Verma, Mai Abdusamad, Jordan Rossen, Lena Joesch-Cohen, Ranad Humeidi, Ryan D. Spangler, John K. Eaton, Evgeni Frenkel, Mustafa Kocak, Steven M. Corsello, Svetlana Lutsenko, Naama Kanarek, Sandro Santagata, Todd R. Golub   +17 more
openaire   +2 more sources

Protein lipoylation: mitochondria, cuproptosis, and beyond

Trends in Biochemical Sciences
Protein lipoylation, a crucial post-translational modification (PTM), plays a pivotal role in mitochondrial function and emerges as a key player in cell death through cuproptosis. This novel copper-driven cell death pathway is activated by excessive copper ions binding to lipoylated mitochondrial proteins, disrupting energy production and causing ...
Ming Tan, Mien-Chie Hung, Robert W Sobol   +2 more
exaly   +3 more sources

Lipoylated Peptides and Proteins

2015
Lipoic acid is a heterocyclic sulfur-containing derivative of octanoic acid that is characterized by a 1,2-dithiolane ring. Found in nature as an essential protein cofactor, lipoic acid is implicated in cellular metabolic reactions. In particular, lipoylation is an essential posttranslational modification involved in cellular energetic metabolism ...
Rentier, Cédric, Pacini, Giulia, NUTI, FRANCESCA, ROVERO, PAOLO, PAPINI, ANNA MARIA   +4 more
openaire   +1 more source

A Lipoate-Protein Ligase Is Required for De Novo Lipoyl-Protein Biosynthesis in the Hyperthermophilic Archaeon Thermococcus kodakarensis

Applied and Environmental Microbiology, 2022
Based on previous studies in bacteria and eukaryotes, lipoate-protein ligases (Lpls) have been considered to be involved exclusively in lipoate salvage. The genetic analyses in this study on the lipoate-protein ligase in T. kodakarensis , however, suggest otherwise and that the enzyme is additionally involved in
Jian-qiang Jin, Takaaki Sato, Shin-ichi Hachisuka, Haruyuki Atomi   +3 more
openaire   +2 more sources

Two redundant octanoyltransferases and one obligatory lipoyl synthase provide protein‐lipoylation autonomy to plastids of Arabidopsis

Plant Biology, 2013
AbstractOctanoyltransferases (LIP2) are important for the lipoylation of several α‐ketoacid decarboxylases and glycine decarboxylase, all of which are essential multienzyme complexes of central metabolism, by attaching de novo‐synthesised octanoyl moieties to the respective target subunits.
R, Ewald, C, Hoffmann, E, Neuhaus, H, Bauwe   +3 more
openaire   +2 more sources

Escherichia coli LipA Is a Lipoyl Synthase:  In Vitro Biosynthesis of Lipoylated Pyruvate Dehydrogenase Complex from Octanoyl-Acyl Carrier Protein

Biochemistry, 2000
The Escherichia coli lipA gene product has been genetically linked to carbon-sulfur bond formation in lipoic acid biosynthesis [Vanden Boom, T. J., Reed, K. E., and Cronan, J. E., Jr. (1991) J. Bacteriol. 173, 6411-6420], although in vitro lipoate biosynthesis with LipA has never been observed.
J R, Miller, R W, Busby, S W, Jordan, J, Cheek, T F, Henshaw, G W, Ashley, J B, Broderick, J E, Cronan, M A, Marletta   +8 more
openaire   +2 more sources