300 Units at 25oC; ~ 600 Units at 37oC
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300 Units at 25oC;
~ 600 Units at 37oC
|Formulation:||In 3.2 M ammonium sulphate|
|Stability:||Minimum 1 year at 4oC. Check vial for details.|
|EC Number:||EC 22.214.171.124 (transferred to EC 126.96.36.199)|
|Synonyms:||formate dehydrogenase; formate:NAD+ oxidoreductase|
|Concentration:||Supplied at ~ 75 U/mL|
|Expression:||Recombinant from Candida boidinii|
Catalyses the reaction:
Formate + NAD+ = CO2 + NADH
|Specific Activity:||~ 1 U/mg (25oC, pH 7.6 on formic acid)|
|Unit Definition:||One Unit of formate dehydrogenase is defined as the amount of enzyme required to convert one µmole of formic acid to NADH + CO2 per minute in the presence of NAD+ in potassium phosphate buffer (41 mM), pH 7.6 at 25oC.|
|Application examples:||Applications for the measurement of formate in the food, fermentation, wine, beverage and dairy industries.|
High purity recombinant Formate dehydrogenase (Candida boidinii) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.
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(Escherichia coli) E-HKGDH - Hexokinase/Glucose-6-phosphate dehydrogenase E-HBDH - 3-Hydroxybutyrate dehydrogenase (prokaryote) E-INDHBS - myo-Inositol dehydrogenase (Bacillus subtilis) E-ICDHBS - Isocitrate dehydrogenase (Bacillus subtilis) E-DLDHLM - D-Lactate dehydrogenase
(Leuconostoc mesenteroides) E-LLDHP - L-Lactate dehydrogenase (Porcine) E-LMDHEC - L-Malate dehydrogenase (Escherichia coli) E-MNHPF - Mannitol dehydrogenase
(Pseudomona fluorescens) E-PGDHEC - 6-Phosphogluconate dehydrogenase
(Escherichia coli) E-XYLMUT - Xylose dehydrogenase + Xylose mutarotase
Muschallik, L., Molinnus, D., Bongaerts, J., Pohl, M., Wagner, T., Schöning, M. J., Siegert, P. & Selmer, T. (2017). Journal of Biotechnology, 258, 41-50.
The gene encoding a putative (R,R)-butane-2,3-diol dehydrogenase (bdhA) from Bacillus clausii DSM 8716T was isolated, sequenced and expressed in Escherichia coli. The amino acid sequence of the encoded protein is only distantly related to previously studied enzymes (identity 33-43%) and exhibited some uncharted peculiarities. An N-terminally StrepII-tagged enzyme variant was purified and initially characterized. The isolated enzyme catalyzed the (R)-specific oxidation of (R, R)- and meso-butane-2,3-diol to (R)- and (S)-acetoin with specific activities of 12 U/mg and 23 U/mg, respectively. Likewise, racemic acetoin was reduced with a specific activity of up to 115 U/mg yielding a mixture of (R,R)- and meso-butane-2,3-diol, while the enzyme reduced butane-2,3-dione (Vmax 74 U/mg) solely to (R,R)-butane-2,3-diol via (R)-acetoin. For these reactions only activity with the co-substrates NADH/NAD+ was observed. The enzyme accepted a selection of vicinal diketones, α-hydroxy ketones and vicinal diols as alternative substrates. Although the physiological function of the enzyme in B. clausii remains elusive, the data presented herein clearly demonstrates that the encoded enzyme is a genuine (R,R)-butane-2,3-diol dehydrogenase with potential for applications in biocatalysis and sensor development.Hide Abstract