Formaldehyde dehydrogenase enzyme

Figure 2. Aerobic catabolism of methylated sulfides (adapted from Kelly, 1988). 1) DMSO reductase (Hyphomicrobium sp.) 2) DMDS reductase (Thiobacillus sp. 3) trimethylsulfonium-tetrahydrofolate methyltransferase (Pseudomonas sp.) 4) DMS monooxygenase 5) methanethiol oxidase 6) sulfide oxidizing enzymes 7) catalase 8) formaldehyde dehydrogenase 9) formate dehydrogenase 10) Calvin cycle for CO2 assimilation (Thiobacillus sp.) 11) serine pathway for carbon assimilation (Hyphomicrobium sp.).

Formaldehyde dehydrogenase catalyzes the oxidation of a number of aldehydes, including formaldehyde, to the corresponding acid. The enzyme is important as it catalyzes the detoxification of formaldehyde, a chemical present in small concentrations in most or all biological tissues. Formaldehyde, as well as other aldehydes, spontaneously condense with amino groups — via a Schiff base linkage — to form a condensation product. This type of condensation product is not desirable, and contributes to a small extent to the various types of damage inflicted upon the proteins of the body. 

Under these conditions a dynamic range between 1 pph and 1.3 ppm can be obtained [322]. Hammerle et al. have described an electrochemical ceU containing the enzyme electrode that can directly operate in the gas phase with a limit of detection of 0.3 ppm and no loss of response during 7 h of operation [323]. Formaldehyde dehydrogenase has also been incorporated into a field-effect transistor for the measurement of catalytically-produced protons and the ENFET incorporated to a sampling system that strips the aldehyde into an aqueous phase [324]. 

Strittmatter P, Ball EG. 1955. Formaldehyde dehydrogenase, a glutadiione-dependent enzyme system. J Biol Chem 213 445-461. 

Two sensitive fluorometric enzymatic methods for the determination of formaldehyde release from wood products were described. These methods were developed using the enzyme formaldehyde dehydrogenase to catalyze the oxidation of formaldehyde to form formic acid and NADH in the presenc of oxidized nicotinamide adenine dinucleotide (NAD ). The increase in NADH, which is directly proportional to the concentration of formaldehyde, is measured fluorometrically at em ... 

The first reported gas phase biosensor was in fact an enzyme-based Pz sensor [58]. Crystals coated with formaldehyde dehydrogenase were used to linearly detect formaldehyde in air from lOppb to 100 ppm. A portable version of the sensor was also developed. The battery-operated instrument contained a digital readout and miniature sampling pump. Weighing just 3 lbs it was used in field for on site analysis. 

Heck H d A, Casanova-Schmitz M, Dodd PB, Schachter EN, Witek TJ, Tosim T (1985) Formaldehyde (CH2O) concentrations in the blood of humans and Fischer-344 rats exposed to CH2O under controlled conditions. Am Ind Hyg Assoc J 46 1-3 Uotila L, Koivusalo M (1974) Formaldehyde dehydrogenase from human liver. Purification, properties, and evidence for the formation of glutathione thiol esters by the enzyme. J Biol Chem 249 7653-7663... 

Methanol is analyzed by GC-FID. In blood it is determined by an enzymic method based on its conversion to formaldehyde by alcohol oxidase and the oxidation of formaldehyde to formic acid by the enzyme formaldehyde dehydrogenase. The presence of a toxic concentration of ethanol may give a high positive value. Methanol in air is estimated by passing 1 -4 L of air over silica gel absorbent, desorbing the analyte into water. 

Cos O, Resina D, Ferrer P et al. (2005) Heterologous production of Rhizopus oryzae lipase in Pichia pastoris using the alcohol oxidase and formaldehyde dehydrogenase promoters in batch and fed-batch cultures. Biochem Eng J 26 86-94 Cowan D (1996) Industrial enzyme technology. TIBTECH 14 177-178... 

The preferred absorption-based methods are those based on enzyme-catalyzed reactions. The absorbance of NADH (340 nm) after addition of creatine amidinohydrolase, sarcosine oxidase, formaldehyde dehydrogenase, and NAD to a creatine-containing solution is proportional to the concentration of creatine present. Creatinine amidohydrolase produces creatine from creatinine. Thus, any assays for creatinine which use creatinine amidohydrolase in the first step can be used for creatine by just leaving out that first step. Conversely, creatine can interfere in those analyses, although creatine is normally present in substantially lower concentrations than creatinine. 

Multi-enzymatic catalysts are recognized as the future generation of biocatalysts. They were particularly designed as enzymes encapsulated into hybrid capsules [129]. It has already been proved that the multi-enzymes organization in a single capsule with separated space enhanced the catalytic capacity of the system. Such an example is the dual biocatalyst of formaldehyde and formate dehydrogenases encapsulated in the capsule lumen/wall. It catalyzed the cascade transformation of CO into formaldehyde [132]. Enzymes co-immobilization in separated spaces of the same cavity exhibited higher formaldehyde yields compared to the free enzyme. Also, the recyclability of the biocatalytic system confirmed the superior mechanical stability [132]. 

The major pathways of metabolism of inhaled formaldehyde are oxidation to formate and incorporation into biological macromolecules via tetra-hydrofolate-dependent one-carbon biosynthetic pathways (Huennekens and Osborne 1959, Koi-VUSALO et al. 1982). The most important pathway for oxidation appears to be that catalysed by formaldehyde dehydrogenase (EC 1.2.1.1), an enzyme that requires both glutathione and NAD as cofactors. UOTiLA and Koivusalo (1974) showed that the true substrate is the hemithioacetal adduct of formaldehyde and glutathione and the product formed is the thiol ester of formic acid, S-formylglutathione. 

The resistance of certain Pseudomonas putida strains to formaldehyde and formaldehyde-releasing compounds is a case of intrinsic resistance attributable to the presence of the constitutive enzyme formaldehyde dismutase in these microbes (Adroer et al., 1990). The stoichiometric dismutation of formaldehyde to methanol and formic acid, known to chemists as Cannizaro s reaction, occurs under physiological conditions in microbe cells in which formaldehyde dismutase is present. Furthermore, if formaldehyde is supplied, this promotes in the cells the formation of formaldehyde dehydrogenase, an enzyme that catalyses the conversion of formaldehyde to formic acid (Kato et al., 1984). 

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