The structure of the yeast
NADH dehydrogenase (Ndil) reveals overlapping binding sites for water- and lipid-soluble substrates.
Phosphoenolpyruvate catabolism involves a substrate-level phosphorylation which produces pyruvate (step E-1, Figure 1), oxidative decarboxylation of pyruvate (step F-1) with 1
NADH production, and acetyl-CoA oxidation to C[O.
In addition to the emission characteristics of key amino acids, the native fluorescence from the enzyme
NADH is also considered for the identification and classification of bacterial strains.
2] la minimizacion de consumo de
NADH y NADPH; y en [C.
NADH dehy drogenase 1 gene sequences compared for species and strains of the genus Echino coccus.
A atividade da ADH foi monitorada no sentido da formacao do etanol (acetaldeido [right arrow] ADH [right arrow] etanol) em meio de reacao contendo tampao TrisHCl 50mM, pH 7,5 para nodulo e fosfato de potassio, pH 7,0 para raizes,
NADH 0,2mM, acetaldeido 5mM e extrato enzimatico (HANSON et al.
NAD and
NADH move hydrogen atoms back and forth with other molecules in the cell, thus helping to maintain balance between oxidation and reduction in the cell.
Using unique reagents from the Yagi group, the Felding team discovered that the balance of key metabolic cofactors processed by complex I-specifically, nicotinamide adenine dinucleotide (NAD+) and
NADH, the form it takes after accepting a key electron in the energy production cycle-was disturbed in aggressive breast cancer cells.
To find out if the balance of NAD+ and
NADH was critical for tumor cell behavior, the team proceeded to insert a yeast gene into cancer cells that caused a shift toward more NAD+.
En la produccion biotecnologica de 1,3-PDO, la segunda etapa enzimatica es
NADH dependiente y genera la especie oxidada [NAD.
NADH oxidase activity was measured by adding cell extract to a mixture containing
NADH.
Small amounts of methaemoglobin are produced continuously but the proportion of total haemoglobin that is present as methaemoglobin is maintained at about 1% by the action of an
NADH dependent methaemoglobin reductase; also called
NADH diaphorase II (Neuwrit and Ponka, 1977) and
NADH ferricynide reductase (Board, 1981) and
NADH cytochrome 65 reductase.
