1887

Abstract

Summary: A second-stage mutant of K12 designated as strain 806 grew faster on -lyxose than the mutant strain 805 previously described. Both mutants produced constitutively a novel enzyme, -mannose isomerase, but strain 806 produced twice as much as strain 805. The enzyme could fortuitously convert -lyxose to -xylulose, which is a normal intermediate in the -xylose catabolic pathway. The purified enzyme consisted of four subunits each with a molecular weight of about 40000. In 0·14 -NaSO, the tetramer dissociated completely into dimers. While the tetramer values for -mannose and -lyxose were 80 mm and 300 mm, respectively, the dimer values for these two sugars were both 300 mm. The amino acid composition of the enzyme was also determined.

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/content/journal/micro/10.1099/00221287-124-1-219
1981-05-01
2021-07-30
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