Salmonella typhimurium was shown to use the gentisate pathway to metabolize m-hydroxybenzoate and gentisate, m-Hydroxybenzoate hydroxylase and gentisate 1,2-dioxygenase were induced by growth on either gentisate or m-hydroxybenzoate. These enzymes were not detected when the bacteria were grown with glucose or glucose and either m-hydroxybenzoate or gentisate. However, both enzymes were induced when the bacteria were grown on succinate with either substrate. The maleylpyruvate isomerase required reduced glutathione and was irreversibly inhibited by N-ethylmaleimide.
Salmonella typhimurium was shown to use the gentisate pathway to metabolize m‐hydroxybenzoate and gentisate. m‐Hydroxybenzoate hydroxylase and gentisate 1,2‐dioxygenase were induced by growth on either gentisate or m‐hydroxybenzoate. These enzymes were not detected when the bacteria were grown with glucose or glucose and either m‐hydroxybenzoate or gentisate. However, both enzymes were induced when the bacteria were grown on succinate with either substrate. The maleylpyruvate isomerase required reduced glutathione and was irreversibly inhibited by N‐ethylmaleimide.
Cell-free extracts of Salmonella typhimurium containing gentisate dioxygenase were immobilized by entrapment in carrageenan and polyacrylamide and adsorption to polyester filters. Carrageenan gels were very porous, and the enzyme was slowly inactivated in polyacrylamide. When adsorbed on polyester the enzyme could be lyophilized and reactivated. Batch reactors charged with the immobilized enzyme converted gentisate to maleylpyruvate with yields of 10-90%.
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