Enzyme Activity Measurement for Formaldehyde Dehydrogenase

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Formaldehyde dehydrogenase (EC 1.2.1.46) is an NAD⁺-dependent enzyme that catalyzes the oxidation of formaldehyde to form formate without the external addition of glutathione. This enzyme is a member of the zinc-containing medium-chain alcohol dehydrogenase (ADH) family, a subgroup of the MDR enzymes. It can be isolated and characterized from both human and bacterial cells such as Ogataea angusta, Methylococcus capsulatus and Pseudomonas putida. The formaldehyde dehydrogenase from P. putida is the most extensively studied among all other sources. It exhibits a homotetramer architecture comprising 398 amino acids for each subunit, with a total molecular mass of 170 kDa. Each subunit consists of seven cysteine residues and two zinc ions which include the catalytic zinc and the structural zinc. The systematic name of this enzyme class is formaldehyde:NAD⁺ oxidoreductase, which is also called NAD⁺-linked formaldehyde dehydrogenase or NAD⁺-dependent formaldehyde dehydrogenase.

Formaldehyde dehydrogenase plays a crucial role in many biological pathways, such as chloroalkane and chloroalkene degradation, methane metabolism and the microbial metabolism in diverse environments. The reaction catalyzed by formaldehyde dehydrogenase is a key part of methane metabolism. Formaldehyde, the substrate of this reaction, is a highly toxic compound and molecular detoxification is a major biochemical necessity for most life forms. Many organisms have developed several oxidation systems to counteract this compound. In the case of methylotrophic bacteria, formaldehyde is not just a toxic compound, but also a central intermediate. As for formate, the other substrate of formaldehyde dehydrogenase, is also a toxic compound. So it can be concluded that formaldehyde dehydrogenase serves as a vital enzyme in many metabolic pathways owing to its ability of degrading these two toxic compounds for most organisms. However, the spectrophotometry-based activity assays of this enzyme have not been well established yet. Fortunately, Creative Enzymes, with many years of experience in enzyme assay development, is able to provide accurate activity assays for this enzyme by tracing the generation of NADH using spectrophotometric quantification at 340 nm. Overall, Creative Enzymes is your best choice which is committed to achieving the highest grade of customer satisfaction, and to constantly improving products, services and quality management system.

Figure: The crystal structure of formaldehyde dehydrogenase from Pseudomonas putida.
PDB: 1KOL