47753
Formate Dehydrogenase from Candida boidinii
liquid (clear), clear brown, 40.0-60.0 U/mL
Synonym(s):
FDH, Formate:NAD+ oxidoreductase
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About This Item
CAS Number:
UNSPSC Code:
12352204
EC Number:
232-844-2
MDL number:
Biological source:
fungus (Candida boidinii)
Concentration:
40.0-60.0 U/mL
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.
Other Notes
Preferred enzyme for regenerating NADH from NAD
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
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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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
Samrat Dutta et al.
The journal of physical chemistry. B, 116(1), 542-548 (2011-12-01)
Functionally relevant femtosecond to picosecond dynamics in enzyme active sites can be difficult to measure because of a lack of spectroscopic probes that can be located in the active site without altering the behavior of the enzyme. We have developed
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