SUMMARY: The transketolase synthesized by CBS 5777 during growth on non-C substrates has been purified and shown to have a molecular weight of approximately 135000 and to consist of two subunits of approximate molecular weight 68000. The enzyme is active with xylulose 5-phosphate as glycolyl donor and ribose 5-phosphate as acceptor; under the conditions of assay formaldehyde was inactive as acceptor. CBS 5777 also synthesizes a second transketolase during growth on methanol. This enzyme, which is unstable, has been purified to homogeneity. It has a wide substrate specificity towards glycolyl donors and acceptors; formaldehyde is a good acceptor and in terms of its physiological role during growth on methanol the enzyme can be described as a dihydroxyacetone synthase. This enzyme has a molecular weight of 105000-110000, with two subunits of molecular weight 62000-67000. Its properties have been compared with analogous enzymes purified elsewhere from methanol-grown KD1 and ( sp.) 2201.


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