Results 181 to 190 of about 3,490 (194)
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Asparagusate dehydrogenases and lipoyl dehydrogenase from asparagus mitochondria
Biochimica et Biophysica Acta (BBA) - Enzymology, 19751. Lipoyl dehydrogenase (NADH: lipoamide oxidoreductase, ED 1.6.4.3) and two asparagusate dehydrogenases from asparagus mitochondria were purified by a series of steps, freezing and thawing, sodium dodecylsulfate extraction, and chromatography on Sephadex G-200 and DEAE-cellulose. 2.
H, Yanagawa, F, Egami
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Characterization of Lipoyl Synthase from Mycobacterium tuberculosis
Biochemistry, 2016The prevalence of multiple and extensively drug-resistant strains of Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis, is on the rise, necessitating the identification of new targets to combat an organism that has infected one-third of the world's population, according to the World Health Organization.
Nicholas D, Lanz +6 more
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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 +3 more
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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 +3 more
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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 +4 more
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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 +4 more
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[32] Assay for protein lipoylation reaction
1995Publisher Summary This chapter discusses the assay for protein lipoylation reaction. Lipoate attaches to the ɛ -amino group of the specific lysine residue of the proteins via an amide linkage. The lipoyllysine residue functions as a carrier of intermediates of the reactions and reducing equivalents between the active sites of the components of the ...
Kazuko Fujiwara +2 more
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A colorimetric method for the assay of lipoyl dehydrogenase
Mikrochimica Acta, 1975A 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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Characterization of a Radical Intermediate in Lipoyl Cofactor Biosynthesis
Journal of the American Chemical Society, 2015Lipoyl synthase (LipA) catalyzes the final step in the biosynthesis of the lipoyl cofactor, the insertion of two sulfur atoms at C6 and C8 of an n-octanoyl chain. LipA is a member of the radical S-adenosylmethionine (SAM) superfamily of enzymes and uses two [4Fe-4S] clusters to catalyze its transformation.
Nicholas D, Lanz +6 more
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[52] Lipoyl dehydrogenase from pig heart
1966Publisher Summary This chapter discusses the determination of lipoyl dehydrogenase from pig heart. Three suitable assays described are: reduced diphosphopyridine nucleotide (DPNH)–lipoyl reductase activity, DPNH–dichlorophenolindophenol reductase activity, and DPNH–ferricyanide reductase activity.
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On the reaction mechanism of lipoyl dehydrogenase
Biochimica et Biophysica Acta, 1960V, MASSEY, C, VEEGER
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