Until about 1957 the L(+)-lactic dehydrogenase of aerobic cells was the only enzyme concerned with lactate oxidation known to occur in yeast. At that time, essentially simultaneously and independently, four laboratories discovered the existence of a second lactic dehydrogenase in yeast, which, in distinction to the L enzyme, occurred in anaerobic cells and reacted with ferricyanide but not cyto...

The aldo-keto reductases metabolize a wide range of substrates and are potential drug targets. This protein superfamily includes aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases and dihydrodiol dehydrogenases. By combining multiple sequence alignments with known three-dimensional structures and the results of site-directed mutagenesis studies, we have developed a structure/...

Information on steroid concentrations in tissues is important for an understanding of the metabolism of these substances and also for diagnostic purposes in certain clinical conditions. Existing procedures for determining steroids, either singly or in mixtures, are based upon calorimetric methods or tedious bioassays. The merits and limitations of these procedures have been critically appraised...

In a previous study, the essential role of 3-sulfinopropionyl coenzyme A (3SP-CoA) desulfinase acyl-CoA dehydrogenase (Acd) in Advenella mimigardefordensis strain DPN7(T) (AcdDPN7) during degradation of 3,3'-dithiodipropionic acid (DTDP) was elucidated. DTDP is a sulfur-containing precursor substrate for biosynthesis of polythioesters (PTEs). AcdDPN7 showed high amino acid sequence similarity t...

Kiese (1) reported the presence of an enzyme in erythrocytes that would catalyze the reduction of methemoglobin by reduced triphosphopyridine nucleotide in the presence of methylene blue. This enzyme was purified further by Huennekens et al. (2) and reported to be active both with TPNH and, to a lesser extent, with DPNH. It was postulated that this enzyme was responsible for the physiological m...

Malate dehydrogenases (MDH, L-malate:NAD oxidoreductase, EC 1.1.1.37), catalyze the NAD/NADH-dependent interconversion of the substrates malate and oxaloacetate. This reaction plays a key part in the malate/aspartate shuttle across the mitochondrial membrane, and in the tricarboxylic acid cycle within the mitochondrial matrix. They are homodimeric molecules in most organisms, including all euka...

Two alcohol dehydrogenases with different catalytic properties were separated from Rhizopus javanicus, and some of their immunological and molecular properties were compared.