PMID:7033464
| Citation |
Stevens, FJ, Stevens, PW, Hovis, JG and Wu, TT (1981) Some properties of D-mannose isomerase from Escherichia coli K12. J. Gen. Microbiol. 124:219-23 |
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| Abstract |
A second-stage mutant of Escherichia coli K12 designated as strain 806 grew faster on D-lyxose than the mutant strain 805 previously described. Both mutants produced constitutively a novel enzyme, D-mannose isomerase, but strain 806 produced twice as much as strain 805. The enzyme could fortuitously convert D-lyxose to D-xylulose, which is a normal intermediate in the D-xylose catabolic pathway. The purified enzyme consisted of four subunits each with a molecular weight of about 40 000. In 0.14 M-Na2SO4, the tetramer dissociated completely into dimers. While the tetramer Km values for D-mannose and D-lyxose were 80 mM and 300 mM, respectively, the dimer Km values for these two sugars were both 300 mM. The amino acid composition of the enzyme was also determined. |
| Links | |
| Keywords |
Aldose-Ketose Isomerases; Amino Acids/analysis; Carbohydrate Epimerases/isolation & purification; Escherichia coli/enzymology; Escherichia coli/genetics; Mutation; Sodium; Substrate Specificity; Sulfates |
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