Enzyme Activity Measurement of NADH Peroxidase

The rigorous approaches to accurate enzyme activity measurement distinguish Creative Enzymes from our competitors. We have provided the best activity measurement to thousands of clients and continue carrying out high-quality services using the most up-to-date instrument. We have extensive experiences on oxidoreductases testing, such as NADH peroxidase, which is measured by precise spectrophotometric assays.

NADH peroxidase (EC 1.11.1.1) is a flavoenzyme using NADH to catalyze the reduction of hydrogen peroxide into water, with FAD as a cofactor. This enzyme belongs to the family of oxidoreductases, especially the ones that employ peroxide as acceptors. NADH peroxidase was original identified by Dolin and subsequently found existing in prokaryotic microorganisms such as Lactobacillus casei and some plants, such as Hordeum vulgare.

The oxidative burst is one of the major mechanisms by which the host’s phagocytes kill pathogenic bacteria. Therefore, an efficient oxidative stress response aiming to increase the cell’s antioxidant defense may be crucial to survival of bacteria. NADH peroxidase potentially defense against externally provided hydrogen peroxide in aerobic growth conditions, through converting it into the water molecular to release the oxidative stress. This enzymatic defense firstly becomes available to protect from the H₂O₂-mediated disinfection. Secondly, the presence of this enzyme provides an additional mechanism to regenerate NAD⁺, which is essential for metabolism and vital in fermentation. In some species, this enzyme also contribute to bacterial virulence. For example, Enterococcus faecalis is well equipped with NADH peroxidase activities, and becomes the pathogen in hospitalized patients with prolonged antibiotic treatments, severe underlying diseases, and the impaired immune system. Although crystal structures from some gram-negative bacteria have been reported, the functions of the enzyme are not yet completely understood. Therefore, the in-depth studies continue to further explore the mechanism and structure of the enzyme. At present, there are only few companies that provide activity measurement for NADH peroxidase. The lack of reliable, large-scale quantification methods would slow down the progress of further studies. Creative Enzymes will be the driving force in industrializing the accurate enzyme assays for the enzyme, which will effectively support your research.

Figure: The crystal structure of NADH peroxidase with cysteine-sulfenic acid.
Reference: Yeh, J.I. et al. Biochemistry 1996 35: 9951-9957.

Creative Enzymes is devoted to providing inspiring services for enzyme activity measurement, which are well welcomed for the high reliability and reproducibility. Creative Enzymes has been enjoying a dominant market share in enzymatic assay services. We look forward to serve more researchers in the future with trustworthy service quality.