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47753

Sigma-Aldrich

Formate Dehydrogenase from Candida boidinii

liquid (clear), clear brown, 40.0-60.0 U/mL

Sinónimos:

FDH, Formate:NAD+ oxidoreductase

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About This Item

Número de CAS:
9028-85-7
Comisión internacional de enzimas:
1.2.1.2 (BRENDA, IUBMB)
EC Number:
232-844-2
MDL number:
MFCD00081614
UNSPSC Code:
12352204

biological source

fungus (Candida boidinii)

form

liquid (clear)

mol wt

Mr ~76000

concentration

40.0-60.0 U/mL

color

clear brown

density

1.1 g/mL at 20 °C

storage temp.

−20°C

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Biochem/physiol Actions

Formate dehydrogenase is involved in the stress response of plants and catalyzes the reduction of NAD+ to NADH.

Unit Definition

1 U corresponds to the amount of enzyme which oxidizes 1 μmol sodium formate (Cat. No. 71539) per minute at pH 7.6 and 25 °C

Other Notes

Preferred enzyme for regenerating NADH from NAD

comparable product

Referencia del producto
Descripción
Precios

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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K. Drauz et al.
Enzyme Catalysis in Organic Synthesis, 597-597 (1995)
Dmitry K Nilov et al.
Journal of biomolecular structure & dynamics, 30(2), 170-179 (2012-06-19)
The formation of the reactive enzyme-substrate complex of formate dehydrogenase has been investigated by molecular dynamics techniques accounting for different conformational states of the enzyme. Simulations revealed that the transport of substrate to the active site through the substrate channel
Sofia Marques da Silva et al.
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 17(5), 831-838 (2012-04-25)
Desulfovibrio spp. are sulfate-reducing organisms characterized by having multiple periplasmic hydrogenases and formate dehydrogenases (FDHs). In contrast to enzymes in most bacteria, these enzymes do not reduce directly the quinone pool, but transfer electrons to soluble cytochromes c. Several studies
Yoshihiro Ojima et al.
Biotechnology letters, 34(5), 889-893 (2012-01-05)
Pyruvate was produced from glucose by Escherichia coli BW25113 that contained formate dehydrogenase (FDH) from Mycobacterium vaccae. In aerobic shake-flask culture (K (L) a = 4.9 min(-1)), the recombinant strain produced 6.7 g pyruvate l(-1) after 24 h with 4 g sodium formate l(-1) and a yield of
C Vinals et al.
Biochemical and biophysical research communications, 192(1), 182-188 (1993-04-15)
We propose a multiple alignment of the sequence of formate dehydrogenase with the D-specific 2-hydroxy acid dehydrogenases family. Structurally conserved regions are predicted for those sequences corresponding to important regions of the catalytic and the coenzyme binding domains defined from
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