Abstract
The utilization of glycerol as a carbon source for growth by Klebsiella aerogenes, strain 2103, involves separate aerobic (sn-glycerol-3-phosphate or G3P) and anaerobic (dihydroxyacetone or DHA) pathways of catabolism. Enzyme and transport activities of the aerobic pathway are elevated in cells grown under oxygenated conditions on glycerol or G3P. Anaerobic growth on G3P as carbon source requires the presence of an exogenous hydrogen acceptor such as fumarate; cells thus grown also are highly induced in the G3P pathway. Anaerobic growth on glycerol requires no exogenous hydrogen acceptors; cells thus grown are highly induced in the DHA pathway but almost uninduced in the G3P pathway and the addition of fumarate electron acceptors has no effect on the relative levels of the two pathways. When both glycerol and G3P are provided anaerobically with fumarate, the DHA pathway is still preferentially induced, which probably accounts for the exclusive utilization of glycerol until its exhaustion. These observations suggest the presence of a regulatory control of G3P pathway imposed by the operation of the DHA pathway.
MeSH Terms
Acetone/metabolism
Aerobiosis
Alcohol Oxidoreductases/metabolism
Alkaline Phosphatase/metabolism
Anaerobiosis
Carbon Radioisotopes
Cell-Free System
Electron Transport
Enzyme Induction
Fumarates/metabolism
Genes
Glycerol/metabolism
Glycerolphosphate Dehydrogenase/metabolism
Glycerophosphates/metabolism
Klebsiella/enzymology,growth & development,metabolism
Membrane Transport Proteins/metabolism
Mutation
Phosphotransferases/metabolism
Chemicals
Carbon Radioisotopes
Fumarates
Glycerophosphates
Membrane Transport Proteins
Acetone
Alcohol Oxidoreductases
Glycerolphosphate Dehydrogenase
Phosphotransferases
Alkaline Phosphatase
Glycerol
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Ruch F E
Lengeler J
Lin E C
References (15)
15 references, click to expand
-
High resolution colony staining for the detection of bacterial growth requirement mutants using naphthol azo-dye techniques.
Biochem Biophys Res Commun. 1965 Oct 26;21(2):182-6
PMID: 4159772
-
Replacement of a phosphoenolpyruvate-dependent phosphotransferase by a nicotinamide adenine dinucleotide-linked dehydrogenase for the utilization of mannitol.
J Bacteriol. 1967 Feb;93(2):642-8
PMID: 4289962
-
Genetic control of L-alpha-glycerophosphate system in Escherichia coli.
J Mol Biol. 1968 Feb 14;31(3):371-87
PMID: 4866330
-
Control of permeation to glycerol in cells of Escherichia coli.
Biochem Biophys Res Commun. 1968 Jul 26;32(2):344-9
PMID: 4876649
-
Anaerobic L- -glycerophosphate dehydrogenase of Escherichia coli: its genetic locus and its physiological role.
J Bacteriol. 1971 Dec;108(3):1224-34
PMID: 4945192
-
Purification and properties of the flavine-stimulated anaerobic L- -glycerophosphate dehydrogenase of Escherichia coli.
J Bacteriol. 1972 Oct;112(1):539-47
PMID: 4562407
-
Importance of facilitated diffusion for effective utilization of glycerol by Escherichia coli.
J Bacteriol. 1972 Nov;112(2):784-90
PMID: 4563976
-
Three kinds of controls affecting the expression of the glp regulon in Escherichia coli.
J Bacteriol. 1973 Sep;115(3):816-23
PMID: 4580569
-
Metabolic pathways of glycerol dissimilation; a comparative study of two strains of Aerobacter aerogenes.
J Bacteriol. 1953 Nov;66(5):611-9
PMID: 13108864
-
Pathways of glycerol dissimilation in two strains of Aerobacter aerogenes; enzymatic and tracer studies.
J Biol Chem. 1957 Jun;226(2):891-9
PMID: 13438878
-
Utilization of L-alpha-glycerophosphate by Escherichia coli without hydrolysis.
Proc Natl Acad Sci U S A. 1962 Dec 15;48:2145-50
PMID: 13930693
-
ACTIVE TRANSPORT OF L-ALPHA-GLYCEROPHOSPHATE IN ESCHERICHIA COLI.
J Biol Chem. 1964 Sep;239:3098-105
PMID: 14217902
-
THE PURIFICATION AND PROPERTIES OF NEUROSPORA MALATE DEHYDROGENASE.
Arch Biochem Biophys. 1965 Mar;109:466-79
PMID: 14320488
-
The effect of aerobic metabolism on the inducible glycerol dehydrogenase of Aerobacter aerogenes.
J Biol Chem. 1960 Jun;235:1824-9
PMID: 14417008
-
Influence of inorganic phosphate in the formation of phosphatases by Escherichia coli.
Biochim Biophys Acta. 1960 Mar 11;38:460-9
PMID: 13838951