
The Biosynthesis of Non-protein Sulfur Amino Acid in Developing Seeds of Common Bean
Abstract
The protein quality of common bean (Phaseolus vulgaris) is associated with the level of dietary essential sulphur amino acids – methionine and cysteine. Extra sulphur that cannot be stored in the protein pool accumulates as the non-protein amino acid S-methylcysteine (S-methylCys) and its dipeptide γ-glutamyl-S-methylcysteine (γ-Glu-S-methylCys). Previous studies have indicated that S-methylhomoglutathione (S-methylhGSH) is present in the developing seed of common bean. It is hypothesized that S-methylhGSH is the key intermediate in the biosynthetic pathway of the γ-Glu-S-methylCys that leads to the accumulation of this dipeptide. This project elucidated the unknown biochemical pathway of S-methylhGSH synthesis using 34S labeled methionine and 13C labeled sodium thiomethoxide in feeding experiments with developing seeds. The results suggest S-methylhGSH is synthesized by methylation of homoglutathione (hGSH). Biochemical assay with seed extract suggested γ-glutamyl transferase (GGT) is likely to catalyzing the reaction between hGSH and S-methylCys to produce γ-Glu-S-methylCys. Furthermore, benzoic acid was identified as the inhibitor for the enzyme catalyzed the synthesis of S-methylCys, BSAS4;1. The findings delineate the biosynthetic pathways of the sulphur metabolome and provide potential approach to improve nutritional quality of common bean.