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In enzymology, a cysteine synthase (EC 2.5.1.47) is an enzyme that catalyzes the chemical reaction. O 3-acetyl-L-serine + hydrogen sulfide L-cysteine + acetate. Thus, the two substrates of this enzyme are O 3-acetyl-L-serine and hydrogen sulfide, whereas its two products are L-cysteine and acetate.
L-cysteine production pathways; Reactants → Enzyme Cofactors Notes O-acetyl-L-serine/hydrogen sulfide → cysteine synthase [9] pyridoxal phosphate not present in humans L-cystine/2 glutathione → glutathione-cystine transhydrogenase [10] cystathionine: → cystathionine γ-lyase [4] pyridoxal phosphate 3-mercapto-pyruvate: → cysteine ...
There are five different structurally related types of PLP enzymes. Members of this family belong to the type I and are: [6] in the transsulfurylation route for methionine biosynthesis: Cystathionine γ-synthase (metB) which joins an activated homoserine ester (acetyl or succinyl) with cysteine to form cystathionine
Cysteine (/ ˈ s ɪ s t ɪ iː n /; [5] symbol Cys or C [6]) is a semiessential [7] proteinogenic amino acid with the formula HOOC−CH(−NH 2)−CH 2 −SH. The thiol side chain in cysteine enables the formation of disulfide bonds, and often participates in enzymatic reactions as a nucleophile. Cysteine is chiral, but both D and L-cysteine ...
The systematic name of this enzyme class is O-acetyl-L-homoserine:methanethiol 3-amino-3-carboxypropyltransferase. Other names in common use include O -acetyl- L -homoserine acetate-lyase (adding methanethiol) , O-acetyl- L -homoserine sulfhydrolase , O -acetylhomoserine (thiol)-lyase , O -acetylhomoserine sulfhydrolase , and methionine synthase .
The plant glutamate cysteine ligase is a redox-sensitive homodimeric enzyme, conserved in the plant kingdom. [26] In an oxidizing environment, intermolecular disulfide bridges are formed and the enzyme switches to the dimeric active state. The midpoint potential of the critical cysteine pair is -318 mV.
In enzymology, a phosphopantothenate—cysteine ligase also known as phosphopantothenoylcysteine synthetase (PPCS) is an enzyme (EC 6.3.2.5) that catalyzes the chemical reaction which constitutes the second of five steps involved in the conversion of pantothenate to Coenzyme A.
The systematic name of this enzyme class is L-cystathionine L-homocysteine-lyase (deaminating; pyruvate-forming). This enzyme participates in 5 metabolic pathways: methionine metabolism, cysteine metabolism, selenoamino acid metabolism, nitrogen metabolism, and sulfur metabolism.