Affiliation:
1. Department of Microbiology, The University of Chicago, Chicago, Illinois 60637
Abstract
Cell-free extracts of
Pasteurella pseudotuberculosis
and
P. pestis
catalyzed a rapid and reversible exchange of electrons between pyridine nucleotides. Although the extent of this exchange approximated that promoted by the soluble nicotinamide adenine dinucleotide (phosphate) transhydrogenase of
Pseudomonas fluorescens
, the reaction in the pasteurellae was associated with a particulate fraction and was not influenced by adenosine-2′-monophosphate. The ability of
P. pseudotuberculosis
to utilize this system for the maintenance of a large pool of nicotinamide adenine dinucleotide phosphate could not be correlated with significant participation of the Entner-Doudoroff path or catabolic use of the hexose-monophosphate path during metabolism of glucose. As judged by the distribution of radioactivity in metabolic pyruvate, glucose and gluconate were fermented via the Embden-Meyerhof and Entner-Doudoroff paths, respectively. With the exception of hexosediphosphatase, all enzymes of the three paths were detected, although little or no gluconokinase or phosphogluconate dehydrase was present unless the organisms were cultivated with gluconate. The significance of these findings is discussed with respect to the regulation of carbohydrate metabolism in the pasteurellae, related enteric bacteria, and
P. fluorescens
.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
17 articles.
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