Diaphorase are dehydrogenase enzymes which catalyze the dehydrogenation of the reduced forms of the co-enzyme NADH and NADPH. NADH and NADPH originally come from purified extracts of Clostridium kluyveri cells, where diaphorase activity is shown. Other diaphorase activities come from various bacteria, plants and mammalian organs. This enzyme was isolated from Bacillus megaterium.
• Used in the reoxidation of NADP to NADPH
• Used to construct a biosensor for acetaldehyde by immobilization
• Used in a study to assess the protein-protein interactions in assembly of lipoic acid on the 2-oxoacid dehydrogenases of aerobic metabolism
• EC 188.8.131.52
• More than 70 U/mg solid
• Isoelectric point: pH 4.2
• Michaelis constant: NADH 5.5x10^-4 M
• Optimum pH: 8.0-9.0
• pH stability: 6.0-9.0 (37 C, 60 min)
• Optimum temperature: 40-45 C
• Thermal Stability: stable at 50 C and below (pH 8.0, 10 min)
Not for human therapeutic use or for medicinal purposes. For research applications only.
|Handling||Follow good laboratory hygiene practices. Wear proper Personal Protective Equipment (PPE) and employ exposure controls as indicated in Section 8. Avoid physical contact. Minimize dust generation during use. Wash hands thoroughly after handling.|