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In the facultative methylotroph  P1 the enzyme transaldolase plays an important role in both the pentose phosphate pathway and in the ribulose monophosphate cycle of formaldehyde fixation.Among gluconate-negative mutants of  P1 strains occurred which also were unable to grow on xylose because they had lost the ability to synthesize transaldolase. Furthermore, this loss of transaldolase activity resulted in decreased growth rates on a number of other “heterotrophic” substrates. Contrary to expectation, these mutants still grew on methylamine and were even able to use gluconate as a carbon source at normal rates provided methylamine was supplied as a nitrogen source. Under these conditions high levels of transaldolase were observed.Partial purification of the transaldolases synthesized by gluconate-grown cells of wild type  P1 and methylamine-grown cells of one of these mutants, strain Art 98, revealed the presence of transaldolase isoenzymes. These enzymes displayed similar kinetics but were very different in heat sensitivity. Functionally these isoenzymes are apparently very similar but their synthesis is regulated differently. One of the enzymes is synthesized constitutively whereas the other is specifically induced during growth on C compounds. Strain Art 98 has lost the ability to synthesize the constitutive transaldolase. It is postulated that the C-induced transaldolase serves to ensure a sufficiently high rate of regeneration of ribulose-5-phosphate during growth on C compounds.

archives of microbiology

Regulation and function of transaldolase isoenzymes involved in sugar and one-carbon metabolism in the ribulose monophosphate cycle methylotroph Arthrobacter P1