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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.
A number of pyridoxal-dependent enzymes involved in the metabolism of cysteine, homocysteine and methionine have been shown to be evolutionary related. [1] These enzymes are tetrameric proteins of about 400 amino-acid residues. Each monomer has an active site, which however requires the N-terminal of another monomer to be completed (salt ...
Function: Amylase is an enzyme that is responsible for the breaking of the bonds in starches, polysaccharides, and complex carbohydrates to be turned into simple sugars that will be easier to absorb. Clinical Significance: Amylase also has medical history in the use of Pancreatic Enzyme Replacement Therapy (PERT). One of the components is ...
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
Other names in common use include: β-thionase, cysteine synthase, L-serine hydro-lyase (adding homocysteine), methylcysteine synthase, serine sulfhydrase, and; serine sulfhydrylase. Methylcysteine synthase was assigned the EC number EC 4.2.1.23 in 1961. A side-reaction of CBS caused this. The EC number EC 4.2.1.23 was deleted in 1972. [7]
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 ...
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.
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 .