Results 151 to 160 of about 4,253 (187)

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 ...
Nolan Bick, Peter Tsvetkov, Mark Fleming   +2 more
exaly   +3 more sources

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Studies on the reaction mechanism of lipoyl dehydrogenase

Biochimica et Biophysica Acta, 1961
Abstract A comparison of the rates of reaction of lipoyl dehydrogenase with dihydrolipoamide, reduced diphosphopyridine nucleotide and oxidized acetyl pyridine diphosphopyridine nucleotide have shown the involvement of the enzyme flavin in the transhydrogenase reaction catalyzed by this enzyme.
V, MASSEY, C, VEEGER
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 ...
Robert W Sobol, Ming Tan, Mien-Chie Hung   +2 more
exaly   +3 more sources

Multiplicity and Origin of Isoenzymes of Lipoyl Dehydrogenase

European Journal of Biochemistry, 1972
Reports in the literature on the number of isoenzymes of lipoyl dehydrogenase in mammalian heart mitochondria vary from 2 to 13 and one report claims that no isoenzymes occur in vivo. The present paper provides evidence that 6 main isoenzymes and 2 minor ones of lipoyl dehydrogenase occur in beef and pig heart, 3 of the main components being associated
W C, Kenney, D, Zakim, P K, Hogue, T P, Singer   +3 more
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A colorimetric method for the assay of lipoyl dehydrogenase

Mikrochimica Acta, 1975
A colorimetric method for the direct assay of lipoyl dehydrogenase is described. Enzyme reaction is stopped by ethanol precipitation. This is followed by the displacement of 1,3-bis(2′-pyridyl)-1,2-diaza-prop-2-ene (PAPHY) from a Pd(II)-PAPHY complex by reduced lipoic acid.
A M, Seet, K T, Lee
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Lipoylation of E2 component

1996
Lipoic acid is a prosthetic group of the acyltransferase (E2) components of the pyruvate, (α-ketoglutarate, and branched chain α-keto acid dehydrogenase complexes, X component (the dihydrolipoamide dehydrogenase-binding protein) of the eucaryotic pyruvate dehydrogenase complex, and H-protein of the glycine cleavage system. The lipoyl moiety is attached
Y. Motokawa, K. Fujiwara, K. Okamura-Ikeda   +2 more
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Determination and properties of erythrocyte lipoyl dehydrogenase

Mikrochimica Acta, 1975
Erythrocyte lipoyl dehydrogenase activity has been determined using the Pd(II)-1,3-bis(2′-pyridyl)1,2-diaza-prop-2-ene colorimetric method. Properties of the red cell enzyme are described and normal values for erythrocyte lipoyl dehydrogenase are given. The possible role of this enzyme in the erythrocytes is discussed.
A M, Seet, K T, Lee
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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 [PDF]

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 ...
Y Motokawa, K Okamura-Ikeda
exaly   +2 more sources

Synthesis and Tribological Investigation of Lipoyl Glycerides

Journal of Agricultural and Food Chemistry, 2014
Lipoyl glycerides were synthesized by enzymatic transesterification of lipoic acid with high-oleic sunflower oil in 2-methyl-2-butanol solvent. The synthesis gave a crude product mixture comprising unreacted lipoic acid, free fatty acids, and several lipoyl glyceride structures of varying lipoic acid substitution.
Girma, Biresaw, Joseph A, Laszlo, Kervin O, Evans, David L, Compton, Grigor B, Bantchev   +4 more
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Octanoylation of the lipoyl domains of the pyruvate dehydrogenase complex in a lipoyl‐deficient strain of Escherichia coli

Molecular Microbiology, 1990
SummaryThe overexpression of a subgene encoding a hybrid lipoyl domain of the dihydrolipoamide acetyltransferase component of the pyruvate dehydrogenase complex of Escherichia coli has previously bee shown to result in the formation of lipoylated an unlipoylated products.
S T, Ali, A J, Moir, P R, Ashton, P C, Engel, J R, Guest   +4 more
openaire   +2 more sources