Name | formaldehyde dehydrogenase |
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Synonyms | ADH 3; ADH 5; ADH5; ADH5 protein; ADHX; Alcohol dehydrogenase 5; Alcohol dehydrogenase class 3 chi chain; Alcohol dehydrogenase class III chi chain… |
Name | formaldehyde |
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CAS | formaldehyde |
PubMed | Abstract | RScore(About this table) | |
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18968517 | Kataky R, Bryce MR, Goldenberg L, Hayes S, Nowak A: A biosensor for monitoring formaldehyde using a new lipophilic tetrathiafulvalene-tetracyanoquinodimethane salt and a polyurethane membrane. Talanta. 2002 Mar 4;56(3):451-8. The screen-printed sensor format comprised a working electrode (WE) modified with platinised carbon, a new lipophilic tetrathiafulvalene-tetracyanoquinodimethane (TTF-TCNQ) salt as mediator, a plasticised polyurethane membrane (TECOFLEX SG80, PU) with anionic sites and the enzyme (formaldehyde dehydrogenase FOH) and co-factor (beta-NAD (+)). |
1(0,0,0,1) | Details |
19463791 | Sahoo R, Bhattacharjee A, Majumdar U, Ray SS, Dutta T, Ghosh S: A novel role of catalase in detoxification of in S. cerevisiae. Biochem Biophys Res Commun. 2009 Aug 7;385(4):507-11. Epub 2009 May 20. Yeast flavohemoglobin (YHB) and glutathione-dependent formaldehyde dehydrogenase (GS-FDH) confers resistance against and related reactive species. |
1(0,0,0,1) | Details |
18082472 | Jerome V, Hermann M, Hilbrig F, Freitag R: A fast method for the quantification of The validated method was successfully applied for monitoring a fed-batch bioprocess (starting volume: 8L, initial hydrochloride concentration: 10 mM) producing a dye-linked formaldehyde dehydrogenase in H. zavarzinii ZV 580. |
in fermentation broths by gas chromatography. J Chromatogr B Analyt Technol Biomed Life Sci. 2008 Jan 1;861(1):88-94. Epub 2007 Dec 4.1(0,0,0,1) | Details |
19716429 | Schroer K, Peter Luef K, Stefan Hartner F, Glieder A, Pscheidt B: Engineering the Pichia pastoris Studying the kinetic properties of oxidase (AOX), formaldehyde dehydrogenase (FLD) and dehydrogenase (FDH) and using the derived kinetic data for subsequent kinetic simulations of formation rates led to the identification of FLD activity to constitute the main bottleneck for efficient recycling via the dissimilation pathway. |
oxidation pathway for improved regeneration during whole-cell biotransformation. Metab Eng. 2010 Jan;12(1):8-17. Epub 2009 Aug 27.1(0,0,0,1) | Details |
19011746 | Staab CA, Hellgren M, Hoog JO: Medium- and short-chain dehydrogenase/reductase gene and protein families : Dual functions of alcohol dehydrogenase 3: implications with focus on formaldehyde dehydrogenase and S-nitrosoglutathione reductase activities. Cell Mol Life Sci. 2008 Dec;65(24):3950-60. By oxidation of HMGSH, the spontaneous adduct of formaldehyde, ADH3 is implicated in the detoxification of formaldehyde. |
1(0,0,0,1) | Details |
17572881 | Ghosh A, Goyal A, Jain RK: Study of The utilization pathway in strain LS2 was deciphered by showing the presence of functional dehydrogenase and formaldehyde dehydrogenase genes. |
-induced phenotypic changes in a novel strain of Acinetobacter lwoffii. Arch Microbiol. 2007 Nov;188(5):533-9. Epub 2007 Jun 16.1(0,0,0,1) | Details |
19460944 | Thompson CM, Sonawane B, Grafstrom RC: The ontogeny, distribution, and regulation of alcohol dehydrogenase 3: implications for pulmonary physiology. Drug Metab Dispos. 2009 Aug;37(8):1565-71. Epub 2009 May 21. Class III alcohol dehydrogenase (ADH3), also termed formaldehyde dehydrogenase or S-nitrosoglutathione reductase, plays a critical role in the enzymatic oxidation of formaldehyde and reduction of nitrosothiols that regulate bronchial tone. |
81(1,1,1,1) | Details |
18003660 | Roy TW, Bhagwat AS: Kinetic studies of Escherichia coli AlkB using a new fluorescence-based assay for DNA demethylation. Nucleic Acids Res. 2007;35(21):e147. Epub 2007 Nov 14. It uses formaldehyde dehydrogenase to convert formaldehyde to and monitors the creation of an analog using fluorescence. |
81(1,1,1,1) | Details |
19304846 | Roca A, Rodriguez-Herva JJ, Ramos JL: Redundancy of enzymes for formaldehyde detoxification in Pseudomonas putida. J Bacteriol. 2009 May;191(10):3367-74. Epub 2009 Mar 20. To determine the contribution of the different gene products to formaldehyde and mineralization, mutants with single and double mutations of formaldehyde dehydrogenases were generated, and the effect of the mutations on formaldehyde catabolism was tested by measuring (14) CO (2) evolution from (14) C-labeled formaldehyde. |
50(0,1,4,5) | Details |
17938908 | Jerome V, Hermann M, Hilbrig F, Freitag R: Development of a fed-batch process for the production of a dye-linked formaldehyde dehydrogenase in Hyphomicrobium zavarzinii ZV 580. Appl Microbiol Biotechnol. 2007 Dec;77(4):779-88. Epub 2007 Oct 16. The dye-linked formaldehyde dehydrogenase (dlFalDH) from Hyphomicrobium zavarzinii ZV 580 processes formaldehyde in a highly selective manner and without need for NAD (P). |
32(0,1,1,2) | Details |
19643682 | Bareket L, Rephaeli A, Berkovitch G, Nudelman A, Rishpon J: Carbon nanotubes based electrochemical biosensor for detection of formaldehyde released from a cancer cell line treated with formaldehyde-releasing anticancer prodrugs. Bioelectrochemistry. 2009 Jul 8. This paper reports the development of an electrochemical biosensor for the detection of formaldehyde in aqueous solution, based on the coupling of the enzyme formaldehyde dehydrogenase and a carbon nanotubes (CNT)-modified screen-printed electrode (SPE). |
31(0,1,1,1) | Details |
18656667 | Demkiv O, Smutok O, Paryzhak S, Gayda G, Sultanov Y, Guschin D, Shkil H, Schuhmann W, Gonchar M: Reagentless amperometric formaldehyde-selective biosensors based on the recombinant yeast formaldehyde dehydrogenase. Talanta. 2008 Aug 15;76(4):837-46. Epub 2008 Apr 24. |
12(0,0,2,2) | Details |
17565589 | Demkiv OM, Paryzhak SY, Gayda GZ, Sibirny VA, Gonchar MV: Formaldehyde dehydrogenase from the recombinant yeast Hansenula polymorpha: isolation and bioanalytic application. FEMS Yeast Res. 2007 Oct;7(7):1153-9. Epub 2007 Jun 12. An enzymatic method for formaldehyde assay based on formaldehyde dehydrogenase was developed and used for testing real samples. |
9(0,0,1,4) | Details |
18585147 | Achmann S, Hermann M, Hilbrig F, Jerome V, Hammerle M, Freitag R, Moos R: Direct detection of formaldehyde in air by a novel NAD+- and -independent formaldehyde dehydrogenase-based biosensor. Talanta. 2008 May 15;75(3):786-91. Epub 2007 Dec 23. |
7(0,0,1,2) | Details |
18378663 | Baerends RJ, de Hulster E, Geertman JM, Daran JM, van Maris AJ, Veenhuis M, van der Klei IJ, Pronk JT: Engineering and analysis of a Saccharomyces cerevisiae strain that uses formaldehyde as an auxiliary substrate. Appl Environ Microbiol. 2008 May;74(10):3182-8. Epub 2008 Mar 31. We demonstrated that formaldehyde can be efficiently coutilized by an engineered Saccharomyces cerevisiae strain that expresses Hansenula polymorpha genes encoding formaldehyde dehydrogenase (FLD1) and dehydrogenase (FMD), in contrast to wild-type strains. |
6(0,0,1,1) | Details |
18174148 | Wilson SM, Gleisten MP, Donohue TJ: Identification of proteins involved in formaldehyde metabolism by Rhodobacter sphaeroides. Microbiology. 2008 Jan;154(Pt 1):296-305. R. sphaeroides xoxF is part of a gene cluster that encodes periplasmic c-type cytochromes, including CycI, isocytochrome c (2) and CycB (a cyt c (553i) homologue), as well as adhI, a glutathione-dependent formaldehyde dehydrogenase (GSH-FDH), and gfa, a homologue of a -formaldehyde activating enzyme (Gfa). |
6(0,0,1,1) | Details |
18835606 | Hilbrig F, Jerome V, Salzig M, Freitag R: Strategy for the isolation of native dehydrogenases with potential for biosensor development from the organism Hyphomicrobium zavarzinii ZV580. J Chromatogr A. 2009 Apr 17;1216(16):3518-25. Epub 2008 Sep 12. A specific formaldehyde dehydrogenase has, e.g., been described for the organism Hyphomicrobium zavarzinii ZV580. In addition two dehydrogenases, a formaldehyde and a dehydrogenase, were found in the cell free extract, which had not been described previously. |
3(0,0,0,3) | Details |
19170879 | Nguyen TT, Eiamphungporn W, Mader U, Liebeke M, Lalk M, Hecker M, Helmann JD, Antelmann H: Genome-wide responses to carbonyl electrophiles in Bacillus subtilis: control of the thiol-dependent formaldehyde dehydrogenase AdhA and proteinase YraA by the MerR-family regulator YraB (AdhR). Mol Microbiol. 2009 Feb;71(4):876-94. Epub 2008 Dec 23. We analysed the global expression profile of Bacillus subtilis to the toxic carbonyls (MG) and formaldehyde (FA). |
2(0,0,0,2) | Details |
18621148 | Hu Y, Khan IA, Dasmahapatra AK: Disruption of circulation by We further analyzed alcohol dehydrogenase (Adh 5 and adh8) and aldehyde dehydrogenase (Aldh9A and Aldh1A2) enzyme mRNAs in the embryos exposed to 400 mM for 24 h. |
promotes fetal alcohol spectrum disorder (FASD) in medaka (Oryzias latipes) embryogenesis. Comp Biochem Physiol C Toxicol Pharmacol. 2008 Sep;148(3):273-80. Epub 2008 Jun 22.1(0,0,0,1) | Details |
17634115 | Resina D, Bollok M, Khatri NK, Valero F, Neubauer P, Ferrer P: Transcriptional response of P. pastoris in fed-batch cultivations to Rhizopus oryzae lipase production reveals UPR induction. Microb Cell Fact. 2007 Jul 16;6:21. In this study, the transcriptional levels of some genes related to the unfolded protein response (UPR) and central metabolism of Pichia pastoris were analysed during batch and fed-batch cultivations using an X-33-derived strain expressing a Rhizopus oryzae lipase under control of the formaldehyde dehydrogenase promoter (FLD1), namely the oxidase gene AOX1, the formaldehyde dehydrogenase FLD1, the protein disulfide isomerase PDI, the KAR2 gene coding for the BiP chaperone, the 26S rRNA and the R. oryzae lipase gene ROL. |
1(0,0,0,1) | Details |
19798499 | Lehr NA, Adomas A, Asiegbu FO, Hampp R, Tarkka MT: WS-5995 B, an antifungal agent inducing differential gene expression in the conifer pathogen Heterobasidion annosum but not in Heterobasidion abietinum. Appl Microbiol Biotechnol. 2009 Oct 2. Treatment with 25 microM WS-5995 B for 2 h resulted in a significant up-regulation of expression of -monophosphate dehydrogenase, phosphoglucomutase and GTPase genes, while the expression of genes encoding for thioredoxin and glutathione dependent formaldehyde dehydrogenase was down-regulated in the sensitive fungal strain. |
1(0,0,0,1) | Details |
19011751 | Persson B, Hedlund J, Jornvall H: Medium- and short-chain dehydrogenase/reductase gene and protein families : the MDR superfamily. Cell Mol Life Sci. 2008 Dec;65(24):3879-94. ADH is a dimeric zinc metalloprotein and occurs as five different classes in humans, resulting from gene duplications during vertebrate evolution, the first one traced to ~500 MYA (million years ago) from an ancestral formaldehyde dehydrogenase line. |
1(0,0,0,1) | Details |
18970030 | Vastarella W, Nicastri R: Enzyme/semiconductor nanoclusters combined systems for novel amperometric biosensors. Talanta. 2005 Apr 30;66(3):627-33. Epub 2005 Jan 5. Formaldehyde dehydrogenase was covalently immobilized onto a protecting membrane, which was stratified on part of the semiconductor nanoparticles modified electrode. The covalent enzyme immobilization has been required to improve the stability of the catalytic oxidation of formaldehyde, which occurs after light stimulation of the semiconductor through the electron/hole recombination. |
1(0,0,0,1) | Details |
18412547 | Staab CA, Alander J, Brandt M, Lengqvist J, Morgenstern R, Grafstrom RC, Hoog JO: Reduction of S-nitrosoglutathione by alcohol dehydrogenase 3 is facilitated by substrate via direct cofactor recycling and leads to GSH-controlled formation of glutathione transferase inhibitors. Biochem J. 2008 Aug 1;413(3):493-504. The present study explored ADH3 (alcohol dehydrogenase 3) in its dual function as GSNOR (GSNO reductase) and glutathione-dependent formaldehyde dehydrogenase. The adduct of formaldehyde, HMGSH (S-hydroxymethylglutathione), was oxidized with a k (cat)/K (m) value approx. 10 times the k (cat)/K (m) value of GSNO reduction, as determined by fluorescence spectroscopy. |
1(0,0,0,1) | Details |
17951632 | Lin-Cereghino J, Lin-Cereghino GP: Vectors and strains for expression. Methods Mol Biol. 2007;389:11-26. Incorporated into expression vectors are selectable markers based on biosynthetic pathway genes, dominant drug resistance, or the P. pastoris formaldehyde dehydrogenase gene (FLD1). |
1(0,0,0,1) | Details |
17543375 | Wu H, Romieu I, Sienra-Monge JJ, Estela Del Rio-Navarro B, Anderson DM, Jenchura CA, Li H, Ramirez-Aguilar M, Del Carmen Lara-Sanchez I, London SJ: Genetic variation in S-nitrosoglutathione reductase (GSNOR) and childhood asthma. J Allergy Clin Immunol. 2007 Aug;120(2):322-8. Epub 2007 Jun 1. S-nitrosoglutathione reductase (GSNOR; also known as alcohol dehydrogenase 5 or formaldehyde dehydrogenase) catalyzes the metabolism of S-nitrosoglutathione (GSNO) and controls intracellular levels of S-nitrosothiols. |
1(0,0,0,1) | Details |
19697421 | Speit G, Neuss S, Schmid O: The human lung cell line A549 does not develop adaptive protection against the DNA-damaging action of formaldehyde. Environ Mol Mutagen. 2009 Aug 20. |
0(0,0,0,0) | Details |