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
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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
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Description
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Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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K. Drauz et al.
Enzyme Catalysis in Organic Synthesis, 597-597 (1995)
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
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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