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Current Protocols in Protein Science, 2017
AbstractThis unit describes a number of methods for modifying cysteine residues of proteins and peptides. A general procedure for alkylation of cysteine residues in a protein of known size and composition with haloacyl reagents or N‐ethylmaleimide (NEM) is presented, and alternate protocols describe similar procedures for use when the size and ...
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AbstractThis unit describes a number of methods for modifying cysteine residues of proteins and peptides. A general procedure for alkylation of cysteine residues in a protein of known size and composition with haloacyl reagents or N‐ethylmaleimide (NEM) is presented, and alternate protocols describe similar procedures for use when the size and ...
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EcoSal Plus, 2008
The synthesis of L-cysteine from inorganic sulfur is the predominant mechanism by which reduced sulfur is incorporated into organic compounds. L-cysteineis used for protein and glutathione synthesis and serves as the primary source of reduced sulfur in L-methionine, lipoic acid, thiamin, coenzyme A (CoA), molybdopterin, and other organic ...
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The synthesis of L-cysteine from inorganic sulfur is the predominant mechanism by which reduced sulfur is incorporated into organic compounds. L-cysteineis used for protein and glutathione synthesis and serves as the primary source of reduced sulfur in L-methionine, lipoic acid, thiamin, coenzyme A (CoA), molybdopterin, and other organic ...
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Cysteine-S-sulphonate as an Intermediate in Microbial Synthesis of Cysteine
Nature, 1960THE synthesis of cysteine in micro-organisms from inorganic sulphur sources has been studied for some time, and the available evidence suggests that sulphate sulphur is reduced to the thiosulphate or sulphide state prior to its introduction into the carbon chain of cysteine1–3, although some investigators have postulated that the formation of sulphur ...
T, NAKAMURA, R, SATO
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A cysteine-selective fluorescent probe for the cellular detection of cysteine
Biomaterials, 2012A series of coumarin fluorophores (1-3), each bearing a double bond conjugated quinoline unit that can undergo a Michael-type reaction with thiol-containing compounds, is reported. These systems, designed to provide so-called turn-on changes in fluorescence response when exposed to thiols, act as fluorescent chemical sensors for cysteine (Cys ...
Hyo Sung, Jung +8 more
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The Effect of Dietary Cysteine Level on Cysteine Metabolism in Rats
The Journal of Nutrition, 1982Male, Sprague-Dawley rats were fed L-amino acid diets that contained 0.4% L methionine and either 0, 0.2% (control), or 2.6% L-cysteine (free base) for 5 or 20 days. Hepatic cysteine dioxygenase activity in rats fed 2.6% cysteine was 5 and 3-times as great as in pair-fed control rats at 5 and 20 days, respectively.
K M, Daniels, M H, Stipanuk
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Brain Research, 1975
Cysteine oxidase, which catalyzes the oxidation of cysteine to the neuroexcitatory and neurotoxic compounds cysteine sulfinic and sulfonic acids, previously has not been studied successfully in brain. Here we report optimal conditions for measuring cysteine oxidase activity in rat brain, describe its regional and subcellular distribution and compare ...
C H, Misra, J W, Olney
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Cysteine oxidase, which catalyzes the oxidation of cysteine to the neuroexcitatory and neurotoxic compounds cysteine sulfinic and sulfonic acids, previously has not been studied successfully in brain. Here we report optimal conditions for measuring cysteine oxidase activity in rat brain, describe its regional and subcellular distribution and compare ...
C H, Misra, J W, Olney
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Cysteine proteinases and metastasis
CANCER AND METASTASIS REVIEW, 1984Cysteine proteinases are a subclass of endopeptidases which require activation by thiol reagents. A tumor cysteine proteinase which appears to be related to lysosomal cathepsin B has been implicated in the ability of tumor cells to invade the extracellular matrix and to metastasize to secondary sites.
B F, Sloane, K V, Honn
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Cysteine Synthase: A Key Enzyme of Cysteine Biosynthetic Pathway
Biochemistry (Moscow)Cysteine is an amino acid essential for normal functioning of living organisms. In bacteria and plants, the main mechanism of cysteine synthesis is the thiolation pathway, the second stage of which is catalyzed by either cysteine synthase A (CysK), if the substrate is inorganic sulfide, or cysteine synthase B (CysM), if the substrate is thiosulfate ...
Evgenii K, Les +4 more
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Degradation of DNA by cysteine
Archives of Biochemistry and Biophysics, 1971Abstract Exposure of DNA solutions to cysteine resulted in degradation of the polydeoxynucleotide. This reaction was inhibited by Na2 EDTA and by sodium citrate. Methylcysteine, mercaptoethanol, serine, and homocysteine did not exhibit this degradative effect. Preincubation of cysteine resulted in a more rapid rate of degradation thus suggesting that
H S, Rosenkranz, S, Rosenkranz
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Conformers of Gaseous Cysteine
Journal of Chemical Theory and Computation, 2009Structures, accurate relative energies, equilibrium and vibrationally averaged rotational constants, quartic and sextic centrifugal distortion constants, dipole moments, (14)N nuclear quadrupole coupling constants, anharmonic vibrational frequencies, and double-harmonic infrared intensities have been determined from ab initio electronic structure ...
Jeremiah J, Wilke +4 more
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