Efficient Conversion of Glycine to L-Serine by a Glycine-Resistant Mutant of a Methylotroph using Co^<2+> as an Inhibitor of L-Serine Degradation

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A glycine-resistant mutant, no. 18,which was not lysed by glycine, was obtained from an L-serine-producing mutant, S395 (temperature-sensitive, O-methylserine-resistant), of a facultative methylotroph, Pseudomonas MS31. The mutant stably produced L-serine from glycine. The properties of the enzymes involved in the synthesis and degradation of L-serine were investigated in the wild-type strain MS31 and the L-serine-producing mutants. Mutant derivation had no effect on the activities of methanol dehydrogenase or serine hydroxymethyltransferase, which are involved in L-serine synthesis. On the other hand, the activity of L-serine dehydratase (SDH), which degrades L-serine, was reduced in the mutants. Cobalt (Co^<2+>) inhibited SDH activity and its addition (6.5 mM) to the L-serine production culture significantly stimulated L-serine accumulation up to 14.9 mg/ml. The results suggest that blocking of SDH is important for the efficient production of L-serine from glycine by methylotrophs.
社団法人日本生物工学会の論文
1987-10-25