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A lysine dehydrogenase-based electrode for biosensing of l-lysine
Biosensors and Bioelectronics, 1992An amperometric biosensor for L-lysine based on the recently isolated enzyme lysine dehydrogenase is described. Immobilization of the enzyme onto a platinum electrode is achieved via entrapment within a gelatin support on a cellulose membrane. Anodic detection (at 0.4 V vs.
Dempsey, E +4 more
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Lysine Infusion in Cystinuria: Theoretical Renal Thresholds for Lysine
Clinical Science, 19731. The renal handling of lysine was studied during the intravenous infusion of a lysine load given in such a way that the plasma lysine concentration was constantly increasing. Theoretical renal thresholds, and maximum rates of renal tubular reabsorption of lysine, have been determined in three normal adults, five homozygous cystinuric patients, and ...
F T, Lester, D C, Cusworth
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Lysine acetyltransferases and lysine deacetylases as targets for cardiovascular disease
Nature Reviews Cardiology, 2019Lysine acetylation is a conserved, reversible, post-translational protein modification regulated by lysine acetyltransferases (KATs) and lysine deacetylases (KDACs; also known as histone deacetylases (HDACs)) that is involved in many cellular signalling pathways and diseases. Studies in animal models have revealed a regulatory role of reversible lysine
Peng Li, Junbo Ge, Hua Li
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Archives of Biochemistry and Biophysics, 1972
Abstract The metabolism of l -lysine, l -pipecolate, and saccharopine was studied in rabbits. The results indicated the existence of the same metabolic pathways as have been delineated in other species. The rabbit differed from the other species studied previously since saccharopine, l -pipecolate, and d -lysine were all readily converted to CO 2
J A, Grove +3 more
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Abstract The metabolism of l -lysine, l -pipecolate, and saccharopine was studied in rabbits. The results indicated the existence of the same metabolic pathways as have been delineated in other species. The rabbit differed from the other species studied previously since saccharopine, l -pipecolate, and d -lysine were all readily converted to CO 2
J A, Grove +3 more
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Amino Acids, 2015
Determining the bioavailability of lysine in foods and feedstuffs is important since lysine is often the first limiting indispensable amino acid in diets for intensively farmed livestock (pigs and poultry) and also in many cereal-based diets consumed by humans.
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Determining the bioavailability of lysine in foods and feedstuffs is important since lysine is often the first limiting indispensable amino acid in diets for intensively farmed livestock (pigs and poultry) and also in many cereal-based diets consumed by humans.
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The path of lysine to pyrrolysine
Current Opinion in Chemical Biology, 2013Pyrrolysine is the 22nd genetically encoded amino acid. For many years, its biosynthesis has been primarily a matter for conjecture. Recently, a pathway for the synthesis of pyrrolysine from two molecules of lysine was outlined in which a radical SAM enzyme acts as a lysine mutase to generate a methylated ornithine from lysine, which is then ligated to
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Journal of the American Chemical Society, 1947
E, KATCHALSKI, I, GROSSFELD, M, FRANKEL
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E, KATCHALSKI, I, GROSSFELD, M, FRANKEL
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Understanding the Function of Mammalian Sirtuins and Protein Lysine Acylation
Annual Review of Biochemistry, 2021Miao Wang, Hening Lin
exaly