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The Mechanism of Cysteine Oxygenation by Cysteine Dioxygenase Enzymes

Journal of the American Chemical Society, 2007
We present here the first density functional theoretic study into the mechanism of cysteine dioxygenation by a model of cysteine dioxygenase enzymes. A large active site model containing the ligands bound to iron plus amino acid residues that are involved in hydrogen bonding interactions with the substrate is used.
Aluri, Swathi, De Visser, Sam P.
openaire   +3 more sources

Cysteine S-conjugates

1987
Publisher Summary This chapter describes the general methods are described for cysteine S-conjugates synthesis and purification with special emphasis on radiolabeled compounds. Synthesis using methanol and sodium methoxide as base is a procedure, adapted from a method for the synthesis of mercapturic acids, can be used for the synthesis of most ...
P, Hayden   +3 more
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Modification of Cysteine

Current Protocols in Protein Science, 1996
AbstractThis unit describes a number of methods for modifying cysteine residues of proteins and peptides by reduction and alkylation procedures. 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 ...
M W, Crankshaw, G A, Grant
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Cysteine-S-sulphonate as an Intermediate in Microbial Synthesis of Cysteine

Nature, 1960
THE 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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Cysteine Proteases

Industrial Enzymes, 2020
Cysteine proteases (CPs) are present in all living organisms. More than twenty families of cysteine proteases have been described (Barrett, 1994) many of which (e.g. papain, bromelain, ficain , animal cathepsins) are of industrial importance.
Z. Grzonka, F. Kasprzykowski, W. Wiczk
semanticscholar   +1 more source

Modification of Cysteine

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 ...
openaire   +2 more sources

Cysteine-derived hydrogen sulfide and gut health: a matter of endogenous or bacterial origin

Current opinion in clinical nutrition and metabolic care, 2019
Purpose of review Hydrogen sulfide (H2S) is produced in the gut from cysteine by epithelial cells and by the intestinal microbiota. Initially considered as a toxic gas, the pleiotropic effects of H2S are now recognized, especially in the colonic mucosa ...
F. Blachier   +2 more
semanticscholar   +1 more source

Determination of cysteine

Analytical Biochemistry, 1963
Abstract A technically easy, sensitive method for specific determination of cysteine was developed. It was based upon the fact that an equimolecular reaction between cysteine and noradrenochrome caused the pink color of the latter to change to yellow, while the pink color remained unchanged or merely faded in the presence of other sulfhydryl ...
openaire   +2 more sources

Biosynthesis of Cysteine

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 ...
openaire   +2 more sources

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