Disease relevance of ND010

• Enzymatic and energetic properties of the aerobic respiratory chain-linked NADH oxidase system in the marine bacterium Pseudomonas nautica [1].

High impact information on ND010

• Efficient hydroxylation at C-7 and transfer of the methyl group from S-adenosylmethionine require both proteins P7 and P8, although P7 alone shows weak C-7 hydroxylase activity and strong cephalosporin-dependent NADH oxidase activity [2].
• Nearly all ice nucleation activity was associated with the outer membrane because the partitioning of 3-ketodeoxyoctonate (a lipopolysaccharide component) and ice nuclei in cell fractions were similar to and opposite that of NADH oxidase (a cytoplasmic membrane component) [3].
• A nitrilotriacetic acid monooxygenase with conditional NADH-oxidase activity [4].
• The NADH oxidase activity was completely inhibited by 60 microM 2-heptyl-4-hydroxyquinoline-N-oxide (HQNO), while the NADH:quinone oxidoreductase activity was about 37% inhibited by 60 microM HQNO [1].
• Although most of the enzymes of L-lactate catabolism were more active in Pseudomonas sp., NADH oxidase activity was about twice as high in Spirillum sp.; and, unlike Pseudomonas sp., the cytochrome c content of this bacterium increased markedly with decreasing D [5].

Associations of ND010 with chemical compounds

• In contrast, 2-oxoglutarate dehydrogenase and succinate dehydrogenase activities were not influenced by D, and NADH oxidase activity increased with D [6].

Analytical, diagnostic and therapeutic context of ND010

• The complemented cio mutant regained the ability to grow on medium containing 1 mM azide, titration of its NADH oxidase activity with cyanide gave a biphasic curve similar to that of the wild-type organism, and the respiration rate returned to normal levels [7].

References