Formate dehydrogenase

Manufactured by Merck Group

Sourced in United States

Formate dehydrogenase is an enzyme that catalyzes the conversion of formate to carbon dioxide. It is commonly used in various laboratory applications, including the determination of formate levels and the production of NADH from NAD+.

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Lab products found in correlation

Dntps, by Takara Bio (3 mentions) Dna polymerase, by Takara Bio (3 mentions) T4 dna ligase, by Takara Bio (3 mentions) Restriction enzyme, by Takara Bio (3 mentions) Ampicillin, by Merck Group (2 mentions) Sodium formate, by Merck Group (2 mentions) Isopropyl 1 thio β d galactopyranoside, by Duchefa Biochemie (2 mentions) Kanamycin, by Duchefa Biochemie (2 mentions) Nicotinamide adenine dinucleotide, by Merck Group (2 mentions) Alcohol dehydrogenase, by Merck Group (1 mentions) Diaphorase, by Merck Group (1 mentions) L lactate dehydrogenase, by Merck Group (1 mentions) H2so4, by Carl Roth (1 mentions) Glutamate dehydrogenase, by Merck Group (1 mentions) Carbonic anhydrase, by Merck Group (1 mentions) Chromium nitrate, by Sinopharm (1 mentions) Copper 2 acetate, by Sinopharm (1 mentions) Trimesic acid, by J&K Scientific (1 mentions) Terephthalic acid, by J&K Scientific (1 mentions) L glutamic acid, by Sinopharm (1 mentions)

Close spelling variants of this product

Formate dehydrogenase from Candida boidinii

10 protocols using formate dehydrogenase

Enzymatic Assay for Metabolite Analysis

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The enzymes alcohol dehydrogenase (ADH, Enzyme Commission number (EC) 1.1.1.1, 310 U mg⁻¹) from Saccharomyces cerevisiae, formate dehydrogenase (FDH, EC 1.2.1.2, 0.49 U mg⁻¹) from Candida boidinii, l-lactate dehydrogenase (l-LDH, EC 1.1.1.27, 174.5 U mg⁻¹) from Bacillus stearothermophilus, d-lactate dehydrogenase (d-LDH, EC 1.1.1.28, 213 U mg⁻¹) from Lactobacillus leichmanii, and diaphorase (DIA, EC 1.8.1.4, 51 U mg⁻¹) from Clostridium kluyveri were purchased from Sigma-Aldrich (St. Louis, MO, USA). Bovine serum albumin (BSA), glutaraldehyde solution (GA) (25% in H₂O), glycerol, potassium ferricyanide (K₃[Fe(CN)₆]), sodium d-lactate, and ethanol standard solution were also supplied by Sigma-Aldrich. Sodium formate, sodium l-lactate, and the cofactor nicotinamide adenine dinucleotide (NAD⁺) were obtained from AppliChem (Darmstadt, Germany). Potassium phosphate buffer (K₂HPO₄, KH₂PO₄) and H₂SO₄ were from Carl Roth GmbH & Co. KG (Karlsruhe, Germany).
All reagents were of analytical grade and were prepared in deionized water. Enzymatic stock solutions (ADH, DIA, FDH, d-LDH and l-LDH, respectively) were prepared in 0.1 mol L⁻¹ potassium phosphate buffer (pH 7.5). The DIA solution was supplemented with 0.5 mmol L⁻¹ flavin adenine dinucleotide.

Pilas J., Yazici Y., Selmer T., Keusgen M, & Schöning M.J. (2018). Application of a Portable Multi-Analyte Biosensor for Organic Acid Determination in Silage. Sensors (Basel, Switzerland), 18(5), 1470.

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Recombinant Protein Production Protocol

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The steroids used in this study were obtained from TCI (Tokyo Chemical Industry Co., Ltd, Japan). Isopropyl-1-thio-β-D-galactopyranoside (IPTG), 1,4-dithiothreitol (DTT), and kanamycin were purchased from Duchefa Bohemie (Korea). Ampicillin, δ-aminolevulinic acid (ALA), NADH, and formate dehydrogenase were purchased from Sigma-Aldrich (Korea). All of the restriction enzymes, DNA polymerase, T4 DNA ligase, and dNTPs were purchased from Takara Bio (Japan). All other high-grade chemical products were obtained from commercially available sources.

Subedi P., Kim K.H., Hong Y.S., Lee J.H, & Oh T.J. (2021). Enzymatic Characterization and Comparison of Two Steroid Hydroxylases CYP154C3-1 and CYP154C3-2 from Streptomyces Species. Journal of Microbiology and Biotechnology, 31(3), 464-474.

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Formate Quantification by Enzymatic Assay

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Formate was measured by enzymatic assay using formate dehydrogenase as previously described [37 (link)] with slight modifications. Samples were diluted 1/10 with deionized water. A reaction solution containing 610 μL of 80 mM sodium phosphate buffer (pH 7.0), 300 μL of 10 mM nicotinamide adenine dinucleotide (NAD⁺; Sigma-Aldrich, USA) and 100 μL of formate dehydrogenase (~1 mg/mL; Sigma-Aldrich) was mixed with 25 μL of the diluted sample solution. After 2.5 h reaction at 37 °C, the absorbance change by formate-dependent NAD⁺ reduction was measured at 340 nm. Formate concentration was calculated based on the absorbance change and a standard curve prepared using sodium formate solutions (Sigma-Aldrich) with various concentrations.

Jo B.H, & Cha H.J. (2015). Activation of formate hydrogen-lyase via expression of uptake [NiFe]-hydrogenase in Escherichia coli BL21(DE3). Microbial Cell Factories, 14, 151.

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Enzymatic Synthesis of Organic Compounds

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Terephthalic acid (99%), trimesic acid (99%), cystamine hydrochloride, and 2,3,4,5,6-pentafluorobenzyl bromide (99%) were purchased from J&K Scientific Ltd. (Beijing, China). Chromium nitrate, copper(II) acetate, and L-glutamic acid were bought from Sinopharm Chemical Reagent Co., Ltd. (Beijing, China). Carbonic anhydrase (CA, bovine red blood cell), formate dehydrogenase (FateDH, lyophilized), and glutamate dehydrogenase (GDH, bovine liver) were provided by Sigma-Aldrich (St. Louis, MO, USA). Nicotinamide adenine quinone dinucleotide (NADH, 98%) was obtained from Aladdin Biotechnology Co., Ltd. (Shanghai, China). CO₂ (>99%) and ¹³CO₂ (>99%) were purchased from Beijing Ruyuan Ruquan Technology Co., Ltd. (Beijing, China). All other chemicals were obtained from Beijing Chemical Factory (Beijing, China). Double-distilled water was used in all experiments.

Li Y., Wen L., Tan T, & Lv Y. (2019). Sequential Co-immobilization of Enzymes in Metal-Organic Frameworks for Efficient Biocatalytic Conversion of Adsorbed CO2 to Formate. Frontiers in Bioengineering and Biotechnology, 7, 394.

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Enzymatic Oxidation of Alcohols

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Formate dehydrogenase from Candida boidinii (FDH, EC.1.2.1.2, homo-dimer, 76 kDa), formaldehyde dehydrogenase from Pseudomonas sp. (FaldDH, EC.1.2.1.46, homo-dimer, 150 kDa), yeast alcohol dehydrogenase (ADH, EC 1.1.1.1, 141 kDa), reduced and oxidized nicotinamide adenine dinucleotide (NADH/NAD⁺, 98 wt%), L-Histidine (99%), glycerol (99%), L-glutamic acid (99%), L-serine (99%), L-arginine (99%), dopamine hydrochloride (DA), poly (ethyleneimine) (PEI), 2,2′-bipyridyl-5,5′-dicarboxylic acid, and dichloro-(penta-methylcyclopentadienyl)rhodium (III) dimer ([Cp*RhCl₂]₂) were purchased from Sigma-Aldrich (St Louis, MO, United States). CO₂ gas (>99.5%) in a cylinder was purchased from Linde Gas (Sweden).

Zhang Z., Wang H., Nie Y., Zhang X, & Ji X. (2022). Natural Deep Eutectic Solvents Enhanced Electro-Enzymatic Conversion of CO2 to Methanol. Frontiers in Chemistry, 10, 894106.

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Glucose Oxidase Activity Assay

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Glucose oxidase (GOx) from Aspergillus niger was purchased from Sigma-Aldrich as a lyophilized solid with an activity of 10 KU. The hydrogen peroxide (H₂O₂), urea hydrogen peroxide (UHP), α-aminolevulinic acid (ALA), ampicillin (Amp), nicotinamide adenine dinucleotide (NADH), catalase, formate dehydrogenase, and sodium formate were obtained from Sigma-Aldrich (Korea). Isopropyl-1-thio-β-D-galactopyranoside (IPTG) and kanamycin were bought from Duchefa Biochemie (Korea). Restriction enzymes were purchased from Takara Clontech (Korea).

Pardhe B.D, & Oh T.J. (2023). Analysis of critical residues for peroxygenation and improved peroxygenase activity via in situ H2O2 generation in CYP105D18. Frontiers in Microbiology, 14, 1296202.

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Synthesis of Bioactive Compounds

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Alpha- and beta-ionone, steroids, and monoterpenoids were purchased from Tokyo Chemical Industry Co., Ltd. (Seoul, Korea). All of the flavonoids used in this study, δ-aminolevulinic acid (ALA), formate dehydrogenase, ampicillin, and NADH were purchased from Sigma-Aldrich (Yongin, Korea). Isopropyl-1-thio-β-D-galactopyranoside (IPTG), 1, 4-dithiothreitol (DTT), and kanamycin were purchased from Duchefa Biochemie (Haarlem, The Netherlands)). Restriction enzymes, T4 DNA ligase, dNTPs, and DNA polymerase were purchased from Takara Bio (Shiga, Japan). All other high-grade chemicals were purchased from available commercial sources.

Subedi P., Do H., Lee J.H, & Oh T.J. (2022). Crystal Structure and Biochemical Analysis of a Cytochrome P450 CYP101D5 from Sphingomonas echinoides. International Journal of Molecular Sciences, 23(21), 13317.

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Enzymatic Reduction of 3-Fluoropyruvate

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A potential reduction of 3-fluoropyruvate to 3-fluoro-2-hydroxypropionate by lactate dehydrogenase (LDH) was measured in vitro using a previously reported protocol [54 (link)]. Nonradioactive 3-fluoropyruvate (14.6 mg) was dissolved in 4 mL of double distilled water containing 10 IU of rabbit muscle LDH (Sigma) and 5.3 IU of formate dehydrogenase (Sigma). The reaction was started by adding NADH to a final concentration of 0.2 mM and sodium formate to a final concentration of 40 mmol. The final volume was adjusted to 5 mL with double distilled water. The reaction was carried out at 37°C for 24 h under constant, gentle shaking at 120 rpm. Then, solution was spun through a 10 kDa filter to remove enzymes, and 3-fluoro-2-hydroxypropionate was detected by HPLC-MS using an Accela U(HPLC) equipped with a Luna Phenomenex 250*4.60 HPLC column and a ThermoScientific LTQ – ORBITRAP – XL fitted an electrospray ionization source working in negative mode.

Van Hée V.F., Labar D., Dehon G., Grasso D., Grégoire V., Muccioli G.G., Frédérick R, & Sonveaux P. (2017). Radiosynthesis and validation of (±)-[18F]-3-fluoro-2-hydroxypropionate ([18F]-FLac) as a PET tracer of lactate to monitor MCT1-dependent lactate uptake in tumors. Oncotarget, 8(15), 24415-24428.

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Benzoic Acid Derivatives Biocatalysis

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Benzoic acid derivatives, 4-methoxybenzoate was purchased from Tokyo Chemical Industry Co., Ltd. (Korea), 2-methoxy benzoate, and 3-methoxybenzoate were purchased from Sigma-Aldrich (Korea), 2,5-dimethoxybenzoate, 3,5-dimethoxybenzoate, 2-amino 6-methoxybenzoate, and 4-methoxycinnamic acid (4MCA) were purchased from Biosynth Carbosynth (China). T4 DNA ligase, DNA polymerase, and dNTPs were available from Takara Bio (Japan). α-aminolevulinic acid (ALA), ampicillin (Amp), nicotinamide adenine dinucleotide (NADH), nicotinamide adenine dinucleotide phosphate (NADPH), catalase, formate dehydrogenase, sodium formate, spinach Fdx, and spinach Fdr were obtained from Sigma-Aldrich (Korea). Isopropyl-1-thio-β-d-galactopyranoside (IPTG) and kanamycin (Km) were bought from Duchefa Bohemie (Korea). Restriction enzymes were procured from Takara Clontech (Korea).

Pardhe B.D., Paudel L., Han S.R, & Oh T.J. (2024). Genomic insight into O-demethylation of 4-methoxybenzoate by a two-component system from Amycolatopsis magusensis KCCM40447. Heliyon, 10(3), e25083.

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Analytical Methods for Biomolecule Quantification

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All chemicals used in the experiment were of analytical reagent (AR) grade.
Creatinine, formate dehydrogenase, 3-(4,5-dimethylthiazol-2yl)-2,5-diphenyltetrazolium bromide (MTT), nicotinamide adenine dinucleotide (NAD + ), oxalate decarboxylase, 1-methoxy-5-methylphenazinium methyl sulfate (PMS), and urea [Co(NH2)2] were obtained from Sigma-Aldrich (St. Louis, MO). Monobasic sodium phosphate (NaH2PO4•2H2O), dibasic sodium phosphate (Na2HPO4), and magnesium sulfate (MgSO4•7H2O) were bought from Panreac (Barcelona, Spain). Ammonium chloride (NH4Cl), calcium chloride (CaCl2•2H2O), citric acid (C6H8O7•H2O), potassium chloride (KCl), sodium chloride (NaCl), sodium oxalate (Na2C2O4), tri-sodium citrate (Na3C6H5•2H2O) and uric acid were bought from Fisher Scientific (Pittsburgh, PA).
Sodium hydrogen carbonate (NaHCO3) was purchased from Merck (Darmstadt, Germany). Whatman No. 1 filter paper was bought from Cole-Parmer (Vernon Hills, IL). All glassware was thoroughly cleaned with freshly prepared 3:1 HCl/HNO3 and rinsed with Milli-Q water prior to use. NAD + was dissolved in phosphate buffer, pH 7.4, whereas sodium oxalate (Na2C2O4) was prepared using a citratephosphate buffer, pH 5.0. Milli-Q water from a Millipore system (R ≥ 18.2 MΩ cm -1 ) was used throughout the experiments.

Worramongkona P., Seeda K., Phansomboon P., Ratnarathorn N., Chailapakul O, & Dungchai W. (2018). A Simple Paper-based Colorimetric Device for Rapid and Sensitive Urinary Oxalate Determinations. Analytical sciences : the international journal of the Japan Society for Analytical Chemistry, 34(1).

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