Enzymatic Production of L-Cysteine with Tryptophan Synthase of Escherichia coli

概要

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Tryptophan synthase of Escherichia coli catalyzes the synthesis of L-cysteine from various β-substituted-L-alanines (e.g., L-serine) and sulfides (e.g., sodium hydrosulfide). Not only L-serine but also O-methyl-L-serine, O-acetyl-L-serine, β-chloro-L-alanine, L-serine O-sulfate, S-methyl-L-cysteine, O-benzyl-L-serine and S-benxyl-L-cysteine could be used as a substrate for L-cysteine synthesis. L-Serine was the best substrate. The rate of L-cysteine formation from L-serine and sodium hydrosulfide with tryptophan synthase was 47% of that of tryptophan formation from L-serine and indole. Under optimum conditions established for L-cysteine production, 114 g/l of L-cysteine was formed in a molar yield of 94% based on L-serine added. Enzymatically synthesized L-cysteine was confirmed to be L-form after isolation and identification of the product.
公益社団法人日本生物工学会の論文
1989-03-25