Carbohydrate Catabolism of Mima polymorpha II. Abortive Catabolism of Glucose

Abstract

Marus, Adrienne (University of Cincinnati, Cincinnati, Ohio), and Emily J. Bell . Carbohydrate catabolism of Mima polymorpha . II. Abortive catabolism of glucose. J. Bacteriol. 91: 2229–2236. 1966.— Mima polymorpha , unable to grow in the presence of glucose as a sole carbon and energy source, is able to obtain supplemental, utilizable energy from the partial catabolism of this substrate. Various enzymes of hexose catabolism have been assayed in this organism and in M. polymorpha M, a mutant obtained by ultraviolet irradiation. The parent strain contains a functional glucose dehydrogenase, glucose-6-phosphate dehydrogenase, diphosphofructoaldolase, and a 2-keto-3-deoxy-6-phosphogluconate aldolase, but is lacking in glucokinase, gluconokinase, 2-ketogluconokinase, and 6-phosphogluconate dehydrogenase. The enzymes present indicate partially functioning hexose diphosphate and Entner-Doudoroff pathways. The absence of kinases explains the inability of the strain to grow on glucose and an absence of 6-phosphogluconate dehydrogenase would indicate the absence of the complete pentose pathway. The mutant strain, M. polymorpha M, possesses, in addition to those enzymes produced by the wild type, both gluconokinase and 6-phosphogluconate dehydrogenase. The presence of the former explains the mutant's ability to grow on glucose, and the presence of the latter indicates a more complete pentose shunt. The supplemental energy obtained from partial glucose catabolism (to gluconic acid) may be obtained from a cytochrome-linked reaction of the glucose dehydrogenase.