Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Dehydrogenase formaldehyde

FaidDH was isolated and purified in an overall yield of 12 % from cell-free extract of Pseudomonas putida C-83 by chromatography on a column of DEAE-cellulose, DEAE-Sephadex A-50, and hydroxyapatite. NAD and especially NADH stabilize the enzyme during storage and against denaturation at high temperatures. [Pg.360]

The molecular mass of the enzyme was estimated to be 150,000 by gel filtration method, and analysis by SDS-polyacrylamide gel electrophoresis indicated that the enzyme was composed of two subunit monomers [86]. [Pg.360]

Kinetic analysis gave Km values of 67 pM for formaldehyde and 56 pM for NAD+, and suggested that the reaction proceeds by a ping-pong mechanism. The enzyme catalyzed the oxidation of formaldehyde accompanied by the stoichiometric reduction of NAD , but no reverse reaction was observed. The crystal structure of FaidDH from Pseudomonas putida (PFDH) has been solved by the multiwavelength anomalous diffraction method using intrinsic zinc ions and has been refined at a 1.65 A resolution (Fig. 9.3) [87]. [Pg.360]


Novel glycerol and formaldehyde selective sensors based on pEI-Sensitive Field Effect Transistors as transducers and Glycerol Dehydrogenase and Formaldehyde Dehydrogenase as biorecognition elements have been developed. The main analytical parameters of the sensors have been investigated and will be discussed. [Pg.303]

MARTINEZ, M.C., ACHKOR, H., PERSSON, B., FERNANDEZ, M.R., SHAFQAT, J., FARRES, J., JORNVALL, H., PARES, X., Arabidopsis formaldehyde dehydrogenase. Molecular properties of plant class III alcohol dehydrogenase provide further insights into the origins, structure and function of plant class P and liver class I alcohol dehydrogenases, Eur. J. Biochem., 1996,241, 849-857. [Pg.29]

BARBER, R.D., DONOHUE, T.J., Function of a glutathione-dependent formaldehyde dehydrogenase in Rhodobacter sphaeroides formaldehyde oxidation and assimilation, Biochemistry, 1998, 37, 530-537. [Pg.29]

This release of formaldehyde can also be quantified by using formaldehyde dehydrogenase, as described above. An alternative way to determine demethylase activity by measuring the amounts of released formaldehyde is the use of the Nash reaction [68, 69]. This method is based on the formation of the colored 3,5-diacetyl-1,4-dihydropyridine by condensation of formaldehyde and acetylacetone in the... [Pg.112]

There are some methods that are specific to HCHO. For example, the Hantzsch reaction of HCHO, collected with a diffusion scrubber, with ammonium acetate, acetic acid, and acetylacetone to form diacetyldihydrolutidine, which is measured using its fluorescence at 470 nm, has been applied to air measurements (Dasgupta et al., 1988, 1990 Kleindienst et al., 1988a,b Lawson et al., 1990 Khare et al., 1997). Reaction with 1,3-cyclohexanedione and ammonium acetate to form a dihydropyridine derivative that is measured by fluorescence has been used in conjunction with a diffusion scrubber (Fan and Dasgupta, 1994). Enzymatic methods have been used in which formaldehyde dehydrogenase catalyzes the oxidation of HCHO to HCOOH in the presence of -nicotinamide adenine dinucleotide, NAD+, which is reduced to NADH. The latter is measured by fluorescence at 450 nm (Lazrus et al., 1988 Ho and Richards, 1990). [Pg.592]

As well as these major application fields, biosensors and analytical techniques should also benefit from the technology. Some examples have already been described. The detection of formaldehyde by a formaldehyde dehydrogenase coated onto a piezoelectric crystal has been performed at the ppm level. Detection of pesticides and organophosphorus compounds at the ppb level has been rendered... [Pg.275]

H. Schutte, J. Flossdorf, H. Sahm, and M.-R. Kuia, Purification and properties of formaldehyde dehydrogenase and formate dehydrogenase from Candida boidinii, Eur. J. Biochem. 1976, 62, 151-160. [Pg.206]

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.). 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.).
Z-N Yang, WF Bosron, TD Hurley. Structure of human %% alcohol dehydrogenase a glutathione-dependent formaldehyde dehydrogenase. J Mol Biol 265 330-343, 1997. [Pg.205]

Uotila, L., and Koivusalo, M, (1996), Expression of formaldehyde dehydrogenase and S-formylglutathione hydrolase activities in different rat tissues, h "Enzymology and Molecular Biology of Carbonyl Metabolism," Vol. 6 (H, Weiner, R. Lindahl, D. Crabb, and T. Ejim, eds.), pp. 365-371. Plenum, New York. [Pg.271]

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. [Pg.836]

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]. [Pg.123]


See other pages where Dehydrogenase formaldehyde is mentioned: [Pg.526]    [Pg.80]    [Pg.347]    [Pg.275]    [Pg.340]    [Pg.21]    [Pg.23]    [Pg.92]    [Pg.316]    [Pg.112]    [Pg.294]    [Pg.294]    [Pg.744]    [Pg.763]    [Pg.521]    [Pg.133]    [Pg.385]    [Pg.99]    [Pg.65]    [Pg.188]    [Pg.222]    [Pg.356]    [Pg.358]    [Pg.307]    [Pg.5134]    [Pg.5134]    [Pg.5157]    [Pg.5157]    [Pg.247]    [Pg.836]    [Pg.836]    [Pg.247]    [Pg.836]    [Pg.122]   
See also in sourсe #XX -- [ Pg.275 ]

See also in sourсe #XX -- [ Pg.358 ]

See also in sourсe #XX -- [ Pg.246 , Pg.836 ]

See also in sourсe #XX -- [ Pg.160 , Pg.479 , Pg.480 ]

See also in sourсe #XX -- [ Pg.256 , Pg.259 ]

See also in sourсe #XX -- [ Pg.155 , Pg.195 , Pg.357 ]

See also in sourсe #XX -- [ Pg.20 , Pg.104 ]

See also in sourсe #XX -- [ Pg.472 ]

See also in sourсe #XX -- [ Pg.522 ]

See also in sourсe #XX -- [ Pg.21 ]




SEARCH



Dehydrogenases formaldehyde dehydrogenase

© 2024 chempedia.info