n-Glucose-6-phosphate dehydrogenase (Zwischenferment) was discovered by Warburg and Christian in 1931 (1, 2). An active preparation was obtained then from horse erythrocytes and in 1932 from the Lebedev juice made from brewers’ yeast (3). Because of its extreme specificity, this enzyme has become an important analytical tool. Various preparations of it have been described, the first being those...

e.g. phosphoglucomutase, glucose 6-phosphate dehydrogenase and fructose 6-phosphate kinase. However, if the reaction occurs distant from the anomeric carbon atom of the substrate the enzymes show no anomeric specificity, e.g. hexokinase, glucokinase and glucose 6-phosphatase (Wurster & Hess, 1974~). A search for enzymes catalysing anomerization reactions leads to the following conclusion. For D...

The metabolism of glucose was examined in several clinical isolates of Neisseria gonorrhoeae. Radiorespirometric studies revealed that growing cells metabolized glucose by a combination on the Entner-Doudoroff and pentose phosphate pathways. A portion of the glyceraldehyde-3-phosphate formed via the Entner-Doudoroff pathway was recycled by conversion to glucose-6-phosphate. Subsequent catabolis...