Search PubMed⌕ Search

Biomedical subjects

R L Anderson

Publications and source records attributed to R L Anderson.

At least 523 records · Page 29Linked to original sources
PubMed1972

Metabolism of gentiobiose in Aerobacter aerogenes.

Cleavage of gentiobiose in cell extracts of gentiobiose-grown Aerobacter aerogenes was dependent on the presence of adenosine 5'-triphosphate (ATP). The enzymes that participate in the overall reaction were shown to be a beta-glucoside kinase, which catalyzes the phosphorylation of gentiobiose with ATP to form gentiobiose monophosphate [6-O-phosphoryl-beta-d-glucopyranosyl-(1 --> 6)-d-glucose], and a phospho-beta-glucosidase, which catalyzes the hydrolytic cleavage of gentiobiose monophosphate to form equimolar amounts of d-glucose and d-glucose 6-phosphate. Although the beta-glucoside kinase was previously shown to catalyze the phosphorylation of many beta-glucosides that serve as growth substrates (i.e., gentiobiose, cellobiose, cellobiitol, salicin, arbutin, methyl beta-d-glucoside, and phenyl beta-d-glucoside), mutant analysis and induction studies indicate that it functions only in the metabolism of gentiobiose, cellobiose, and cellobiitol.

Adenosine Triphosphate↗
PubMed1972

Evidence for vectorial phosphorylation of D-fructose by intact cells of Aerobacter aerogenes.

Extracellular d-fructose was metabolized preferentially over intracellular d-fructose in growing cells of a d-fructokinaseless mutant of Aerobacter aerogenes. This finding is interpreted to indicate that phosphorylation of d-fructose by the membrane-bound phosphoenolpyruvate: d-fructose 1-phosphotransferase system in intact cells is coupled to unidirectional transport.

Biological Transport, Active↗
PubMed1971

Sorbitol metabolism in Aerobacter aerogenes.

Sorbitol (d-glucitol) metabolism in Aerobacter aerogenes PRL-R3 is shown to proceed via the pathway: sorbitol --> sorbitol 6-phosphate --> d-fructose 6-phosphate. Sorbitol phosphorylation is mediated by a phosphoenolpyruvate (PEP):sorbitol 6-phosphotransferase system, and sorbitol 6-phosphate oxidation by a pyridine-nucleotide-linked dehydrogenase. Mutants deficient in sorbitol 6-phosphate dehydrogenase or a component (enzyme I) of the phosphotransferase system did not grow on sorbitol, whereas revertants which had regained these enzymatic activities grew normally. Extracts of the enzyme I-deficient mutant failed to catalyze the phosphorylation of sorbitol in the presence of PEP, and adenosine 5'-triphosphate could not replace the PEP requirement for sorbitol phosphorylation in extracts of the wild-type strain.

Adenosine Triphosphate↗
PubMed1970

Enzyme replacement in Fabry's disease, an inborn error of metabolism.

Two patients with Fabry's disease were infused with normal plasma to provide active enzyme (ceramide trihexosidase) for hydrolysis of the plasma substrate, galactosylgalactosylglucosylceramide. Maximum ceramide trihexosidase activity occurred 6 hours after infusion of the plasma, attaining a level approximately 150 percent of that in normal plasma; enzymatic activity was detectable for 7 days. The amount of accumulated substrate in the plasma of these recipients decreased about 50 percent on day 10 after infusion. Thus, periodic replacement of ceramide trihexosidase activity in the plasma of patients with Fabry's disease might lead to consistently lower amounts of substrate in the plasma and a decrease in its rate of accumulation in tissues.

Adolescent↗