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Metabolism of D-arabinose by Aerobacter aerogenes: purification of the isomerase.
In Aerobacter aerogenes, the mutational event permitting the utilization of d-arabinose as a source of carbon and energy is a regulatory mutation resulting in the constitutive synthesis of certain… Expand
Enzyme activity in cryobiological systems. II. Identification of cold-stable glyceraldehydephosphate dehydrogenases in certain invertebrates.
Abstract Glyceraldehydephosphate dehydrogenases (GPDHs) purified from a number of sources were examined for their resistance to inactivation at 0 °C by adenosine triphosphate (ATP). In contrast to… Expand
Unusual kinetic transition in honeybee glyceraldehyde phosphate dehydrogenase.
Growth of Aerobacter aerogenes on D-arabinose: origin of the enzyme activities.
Mutants of Aerobacter aerogenes can be selected which are capable of utilizing d-arabinose as a sole source of carbon and energy for growth. Mutants can also be selected which are capable of using… Expand
Regulation of pentitol metabolism by aerobacter aerogenes. II. Induction of the ribitol pathway.
The incubation of Aerobacter aerogenes PRL-R3 with ribitol resulted in the induction of ribitol dehydrogenase and d-ribulokinase, coordinately controlled enzymes of the pathway of ribitol catabolism.… Expand
D-Ribulose production by a mutant of Aerobacter aerogens.
- E. J. Oliver, T. M. Bisson, D. Leblanc, R. P. Mortlock
- Biology, Medicine
- Analytical biochemistry
- 1 February 1969
Abstract A mutant of Aerobacter aerogenes which is ribitol dehydrogenase constitutive and d -ribulokinase deficient has been utilized for the oxidation of ribitol to d -ribulose. The yield of d… Expand
Enzyme activity in cryobiological systems. 3. Low-temperature properties of honeybee glyceraldehydephosphate dehydrogenase.
Abstract Certain properties of honeybee and rabbit muscle GPDHs have been examined in vitro. While incubation of rabbit muscle GPDH at 0 °C in the presence of 4 m m ATP results in its dissociation,… Expand
Competitive inhibition of an L-fucose isomerase activity by dithiothreitol.
Abstract Dithiothreitol was found to be a competitive inhibitor for a purified L-fucose isomerase from Aerobacter aerogenes , inhibiting enzyme activity for the isomerization of both L-fucose and… Expand