Abstract
Cell-free extracts of D-fructose grown cells of Pseudomonas putida, P. fluorescens, P. aeruginosa, P. stutzeri, P. mendocina, P. acidovorans and P. maltophila catalyzed a P-enolpyruvate-dependent phosphorylation of D-fructose and contained 1-P-fructokinase activity suggesting that in these species fructose-1-P and fructose-1,6-P2 were intermediates of D-fructose catabolism. Neither the 1-P-fructokinase nor the activity catalyzing a P-enolpyruvate-dependent phosphorylation of D-fructose was present in significant amounts in succinate-grown cells indicating that both activities were inducible. Cell-free extracts also contained activities of fructose-1,6-P2 aldolase, fructose-1,6-P2 phosphatase, and P-hexose isomerase which could convert fructose-1,6-P2 to intermediates of either the Embden-Meyerhof pathway or Entner-Doudoroff pathway. Radiolabeling experiments with 1-14C-D-fructose suggested that in P. putida, P. aeruginosa, P. stutzeri, and P. acidovorans most of the alanine was made via the Entner-Doudoroff pathway with a minor portion being made via the Embden-Meyerhof pathway. An edd- mutant of O. putida which lacked a functional Entner-Doudoroff pathway but was able to grow on D-fructose appeared to make alanine solely via the Embden-Meyerhof pathway.
MeSH Terms
Alanine/biosynthesis
Fructose/metabolism
Gluconates
Hydro-Lyases/analysis
Mutation
Phosphoenolpyruvate
Phosphofructokinase-1/analysis
Phosphogluconate Dehydrogenase/analysis
Phosphotransferases/analysis
Pseudomonas/enzymology
Chemicals
Gluconates
Fructose
Phosphoenolpyruvate
Phosphogluconate Dehydrogenase
Phosphotransferases
Phosphofructokinase-1
Hydro-Lyases
Alanine
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Sawyer M H
Baumann P
Baumann L
Berman S M
Cánovas J L
Berman R H
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