Abstract
Cell-free preparations of Acetobacter melanogenum readily oxidized glucose-6-phosphate, glucose-1-phosphate, fructose-6-phosphate, 6-phosphogluconate, and ribose-5-phosphate; fructose-1,6-diphosphate was utilized very slowly. The presence of an active triphosphopyridine nucleotide (TPN)-linked glucose-6-phosphate dehydrogenase and of phosphohexose isomerase was demonstrated; phosphoglucomutase was also present in these extracts. 6-Phosphogluconate dehydrogenase activity (TPN-linked) was low in extracts of glucose-grown cells, but was high in sonates of gluconate-grown cells. An active oxidizing system for reduced diphosphopyridine nucleotide was present but transhydrogenase was not detected. Pyruvate was produced extensively from 6-phosphogluconate but only slowly from ribose-5-phosphate; fluoride inhibited pyruvate formation from both substances. Ribose-5-phosphate was degraded readily via the transketolase-transaldolase series of reactions. Glyceraldehyde-3-phosphate dehydrogenase, hexokinase, gluconokinase, 2-ketogluconokinase, and aldolase were detected but not phosphohexokinase. The results suggest that glucose is oxidized either directly or after phosphorylation but is not metabolized glycolytically. The oxidation of hexose phosphate appears to occur predominantly as a result of the splitting of 6-phosphogluconate to pyruvate and glyceraldehyde-3-phosphate.
Publisher
Canadian Science Publishing
Subject
Genetics,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Immunology,Microbiology
Cited by
16 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献