Abstract
Cysteine and methionine are sulphur-containing amino acids in the twenty protein amino acids. The inorganic sulphur, which is an essential nutrient for plants, is first fixed into cysteine by the cysteine biosynthetic pathway. Cysteine is then incorporated into proteins and glutathione or serves as the sulphur donor of methionine and sulphur-containing secondary products in plants. The cysteine biosynthetic pathway involves several enzymatic reactions. The final step of cysteine biosynthesis is the reaction incorporating sulphide moiety into β-position of alanine. The amino acid moiety is derived from serine through O-acetyl-L-serine. Serine acetyltransferase and cysteine synthase (O-acetylserine (thiol)-lyase) are committed in this final step of cysteine biosynthesis. The feedback inhibition for serine acetyltransferase activity plays one of the major roles in regulating cysteine synthesis. Methionine is synthesized from cysteine and O-phosphohomoserine, which is derived from aspartic acid through a pathway involving trans-sulphuration reaction. Three enzymes, cystathionine γ-synthase, cystathionine β-lyase and methionine synthase, are involved in the methionine biosynthesis from cysteine. The methionine biosynthesis is controlled by supply of O-phosphohomoserine and the enzyme, cystathionine γ —synthase.
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Noji, M., Saito, K. (2003). Sulphur Amino Acids: Biosynthesis of Cysteine and Methionine. In: Abrol, Y.P., Ahmad, A. (eds) Sulphur in Plants. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-0289-8_7
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DOI: https://doi.org/10.1007/978-94-017-0289-8_7
Publisher Name: Springer, Dordrecht
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