Fructose-bisphosphate aldolase (EC 4.1.2.13) is a key enzyme in glycolysis. We have characterized full-length coding sequences for aldolase genes from the cyst nematodes Heterodera glycines and Globodera rostochiensis, the first for any plant-parasitic nematode. Nucleotide homology is high (83% identity), and the respective sequences encode 40 kDa proteins with 89% amino acid identity. Genomic ...

Enzyme inactivation was utilized to study subunit interaction in the homotetrameric glycolytic enzyme, aldolase. Isoenzymes from rabbit liver and skeletal muscle were inactivated in the presence of Pi and d-glyceraldehyde-P to a maximum stoichiometry of one modification per aldolase subunit. Subunit modification increased net negative charge on each subunit surface and was used to resolve modif...

Increased nutrient uptake is a major hallmark of cancer and correlates with a poor survival rate. Many of the oncogenic events that drive cancer development influence metabolism by increasing glucose and glutamine uptake while other genetic events and processes also influence metabolism without increased nutrient uptake. Together these events reprogram metabolism away from catabolic metabolism ...

Hereditary fructose intolerance (HFI, OMIM 22960), caused by catalytic deficiency of aldolase B (fructose-1,6-bisphosphate aldolase, EC 4.1.2.13), is a recessively inherited condition in which affected homozygotes develop hypoglycaemic and severe abdominal symptoms after taking foods containing fructose and cognate sugars. Continued ingestion of noxious sugars leads to hepatic and renal injury ...

Two D-ketohexose 1,6-diphosphate aldolases are present in Streptococcus cremoris E8 and S. lactis C10. One aldolase, which was induced by growth on either lactose or galactose, was active with both tagatose 1,6-diphosphate (TDP) and fructose 1,6-diphosphate (FDP), having a lower Km and a higher Vmax with TDP as the substrate. This enzyme, named TDP aldolase, had properties typical of a class I ...

The fructose-1,6-bisphosphate aldolase (EC 4.1.2.13) homotetramer has been destabilized by site-directed mutagenesis at the two different subunit interfaces. A double mutant aldolase, Q125D/E224A, sediments as two distinct species, characteristic of a slow equilibrium, with velocities expected for the monomer and tetramer. The aldolase monomer is shown to be catalytically active following isola...

A single fructose1,6-bisphosphate (FBP) aldolase has been detected in extracts from carrot storage roots (Daucus carota L.). The enzyme was purified 850-fold to electrophoretic homogeneity and a final specific activity of 26.3 amol of FBP utilized/min per mg of protein. SDS/PAGE of the final preparation revealed a single protein-staining band of 40 kDa. The native molecular mass was determined ...

Crystalline fructose diphosphate aldolase preparations obtained from rabbit muscle and bovine liver differ in catalytic efficiency (fructose diphosphate cleavage activity of muscle aldolase is about 10 times that of the liver enzyme) and substrate specificity (the fructose diphosphate to fructose l-phosphate activity ratio is 50 for muscle and 1 for liver aldolase) (2). In spite of these distin...

Both the Schiff base-mediated 2-keto-4-hydroxyglutarate aldolase of liver and the metal-activated a-keto-/3-deoxyhexarate aldolase of Escherichia coli condense pyruvate and glyoxylate to form (4-RS)-Z-keto-4-hydroxyglutarate. Both enzymes catalyzed a condensation between [3-3H3]pyruvate and glyoxylate. It was found that C-C synthesis occurred 6 to 7 times faster than C-T bond cleavage. Thus, py...

1. The contents of dihydroxyacetone phosphate, fructose diphosphate, pyruvate and lactate and the activities of aldolase and lactate dehydrogenase in the liver, kidney, testis, skeletal muscle, blood cells, sarcoma and hepatoma of rats were measured. 2. Correlations were established between components of the glycolytic pathway as follows: activities of aldolase and lactate dehydrogenase; conten...