A New Enzymatic Reaction for Producing New-Type Amino Acids by Escherichia coli : : Production of α-Amino-β-(1-Indoline) Propionic Acid from Indoline and L-Serine

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We found that some reaction products were produced from indole-mimic compounds, such as indoline (2,3-dihydroindole), indazole, 7-azaindole and 3-indazolinone, with L-serine by the catalytic action of the lyophilized cells of Escherichia coli T4-3 (a mutant defective in indole-3-glycerolphosphate synthase [EC 4.1.1.48]) cultured in a tryptophan-limited medium.A main product from indoline and L-serine was isolated and identified as α-amino-β-(1-indoline) propionic acid (AIP) from data obtained by paperchromatography, elemental analysis, UV, IR, ^1H-NMR, ^<13>C-NMR and mass spectrometry.The reaction conditinos and the requirements for the reaction were also studied.AIP was produced only in the case of using L-serine, L-serine methylester and L-serine ethylester as the amino acid source.On the enzyme concerned AIP production, studies were carried out by using the mutant strains of E. coli defective in the enzyme(s) of tryptophan operon. Tryptophan synthase [EC 4.2.1.20], particularly its B protein, was presumed to be a possible candidate.
公益社団法人日本生物工学会の論文
1987-08-25