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Formaldehyde Dehydrogenase

Official Full Name
Formaldehyde Dehydrogenase
Formaldehyde dehydrogenase catalyzes the conversion of formaldehyde to formate.
EC; Formaldehyde Dehydrogenase; NAD-linked formaldehyde dehydrogenase; NAD-dependent formaldehyde dehydrogenase; 9028-84-6

Product Name
EC No.
CAS No.9028-84-6
CAS No.9028-84-6
SourcePseudomonas sp.
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Formaldehyde dehydrogenase (FADH) is a member of the medium zinc chain alcohol dehydrogenase family. It exists in most prokaryotes and all eukaryotes. It is an enzyme mainly used for formaldehyde detoxification in microorganisms. In recent years, some studies have determined that formaldehyde dehydrogenase also has the activity of S-nitrosoglutathione reductase (GSNOR), which is used to regulate the dynamic balance of endogenous NO.

Structure of formaldehyde dehydrogenase Figure 1. Structure of formaldehyde dehydrogenase.


Formaldehyde is an active compound that can react non-specifically with proteins, nucleic acids and lipids, and is highly toxic to all organisms. The source of formaldehyde is very wide. In order to prevent the lethal and mutagenic effects of formaldehyde on organisms, organisms have established a variety of repair mechanisms to enable them to survive better in an environment containing formaldehyde. Among them, the oxidation pathway of formaldehyde is widespread in microorganisms. A way of detoxification. The key enzyme formaldehyde dehydrogenase that acts on this pathway is a member of the medium zinc chain alcohol dehydrogenase family. It exists in most prokaryotes and all eukaryotes, and plays an important role in the detoxification of microbial formaldehyde. In recent years, more and more studies have shown that FADH is not only used for the detoxification of formaldehyde, but also has some connection with NO metabolism, showing S-nitrosoglutathione reductase activity.

Physiological role of formaldehyde dehydrogenase

Biochemical properties

Structure of formaldehyde dehydrogenase

SDS-PAGE analysis revealed that the molecular weights of FADH subunits were all around 40 kD, and gel filtration chromatography showed that there were dimers and tetramers. Studies have found that the formaldehyde dehydrogenases in Escherichia coli and Rhodobacter sphaeroides are usually dimeric proteins, while Pseudomonas putida, Paracoccus denitrificans, yeasts and Sulfolobus sulphureus are in the form of tetramers. The monomer structure of GSH-dependent FADH is basically similar whether it is dimer or tetramer, while GSH-independent FADH has a different structure.

FADH gene expression regulation

The transcription of FADH-encoding genes can be activated by intermediates accumulated in the process of formaldehyde metabolism and signal molecules generated by reducing power in the pathway. Studies have found that Escherichia coli and Haemophilus influenzae can induce the production of FADH enzyme activity at a formaldehyde concentration of 0.6-20 ppm; at the same time, it has also been found in the gram-negative bacteria Paracoccus denitrificans, when its growth substrate is one carbon Compounds can induce the production of FADH enzyme activity, but not when the substrate is methanol or formic acid, indicating that FADH is inducible.



Formaldehyde dehydrogenase exists in most prokaryotes and all eukaryotes. Formaldehyde dehydrogenases from different sources show a high degree of sequence similarity. The conservative existence of formaldehyde dehydrogenase indicates its important role in organisms. The formaldehyde oxidation pathway of formaldehyde dehydrogenase action is a detoxification system widely existing in organisms.

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