L-Lactaldehyde is a branching point in the metabolic pathway of L-fucose and L-rhamnose utilization. Under aerobic conditions, L-lactaldehyde is oxidized to L-lactate by the enzyme lactaldehyde dehydrogenase, while under anaerobic conditions, L-lactaldehyde is reduced to L-1,2-propanediol by the enzyme propanediol oxidoreductase. Aerobic growth on either of the methyl pentoses induces a lactald...

Accurate protein function prediction is an important subject in bioinformatics, especially wheresequentially and structurally similar proteins have different functions. Malate dehydrogenaseand L-lactate dehydrogenase are two evolutionary related enzymes, which exist in a widevariety of organisms. These enzymes are sequentially and structurally similar and sharecommon active site residues, spati...

Lactate dehydrogenase (LDH) is a key enzyme involved in the process of glycolysis, assisting cancer cells to take glucose and generate lactate, as well suppress evade...

Abnormal electrophoretic pattern of serum lactate dehydrogenase isoenzyme is shown. In this case electrophoretic pattern showed a sharp single band between lactate dehydrogenase 4 and lactate dehydrogenase 5 and broad band between lactate dehydrogenase 2 and lactate dehydrogenase 4. This abnormality was suggested to be caused by the presence of lactate dehydrogenase and immunoglobulin G (kappa ...

The transcriptional regulator SugR from Corynebacterium glutamicum represses genes of the phosphoenolpyruvate-dependent phosphotransferase system (PTS). Growth experiments revealed that the overexpression of sugR not only perturbed the growth of C. glutamicum on the PTS sugars glucose, fructose, and sucrose but also led to a significant growth inhibition on ribose, which is not taken up via the...

The Connecticut Department of Public Safety laboratory recently addressed a legal challenge to a hospital alcohol dehydrogenase (ADH)-based serum ethanol determination based on the suggestion of interference by lactate dehydrogenase (LDH)-catalyzed oxidation of lactate. Both ADH- and LDH-oxidations require NAD(+) (present in excess in the assay). NADH produced by LDH-catalyzed lactate oxidation...

The amino-acid sequence of the hemebinding region of bakers' yeast cytochrome b(2) [L-(+)-lactate dehydrogenase, EC 1.1.2.3] has been determined. It shows a strong similarity with the sequence of microsomal cytochrome b(5), and appears to be compatible with the same kind of peptide-chain folding, in agreement with data obtained previously by various physiochemical methods. The comparison shows ...

The aim of this study was to determine the effect of endurance training on the relationship between mechanical stride descriptors (stride rate and stride rate variability) and the aerobic energy cost that would be decreased by training in an all-out supra-lactate threshold run. Six long distance runners (175 +/- 6 cm; 72 +/- 9 kg; 27 +/- 4 years) performed two identical track tests before and a...

In all vertebrates, including humans, the L-lactate form is by far the most abundant and pathophysiologically significant, and it is this form that is specifically measured by the lactate sensors in blood gas analyzers and indeed all routine methods used to measure lactate in the clinical laboratory. The main focus of this brief review is physiological and pathological aspects that distinguish ...