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F8649

Sigma-Aldrich

Formate Dehydrogenase from Candida boidinii

lyophilized powder, 5.0-15.0 units/mg protein

Synonym(s):

FDH, Formate:NAD+ oxidoreductase

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

fungus (Candida boidinii)

form

lyophilized powder

specific activity

5.0-15.0 units/mg protein

composition

Protein, 5.0-20.0% biuret

storage temp.

2-8°C

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Application

Formate Dehydrogenase (FDH) is used for diagnostics in large scale industrial processes. Its used in the production of an unnatural amino acid, tert-L-leucine, a component of some HIV protease and matrix metalloprotease inhibitors.

Biochem/physiol Actions

Formate dehydrogenase is an abundant enzyme from yeast Candida boidinii (CbFDH) that plays an important role in the energy supply of methylotrophic microorganisms and in the stress response of plants.
Formate dehydrogenase is involved in the stress response of plants and catalyzes the reduction of NAD+ to NADH.

Unit Definition

One unit will oxidize 1.0 μmole of formate to CO2 per min in the presence of β-NAD at pH 7.6 at 37 °C.

Pictograms

Health hazard

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

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Held in police custody.
A Skelt
Nursing times, 84(4), 50-52 (1988-01-02)
Do reactive oxygen species or does oxygen itself confer obligate anaerobiosis? The case of Bacteroides thetaiotaomicron.
Khademian, et al.
Molecular Microbiology, 114, 333-347 (2021)
Jana Löwe et al.
Scientific reports, 8(1), 10436-10436 (2018-07-12)
A biotechnological process is reported, which enables an enzymatic reduction without the need for addition of an organic co-substrate for in situ-cofactor recycling. The process is based on merging the fields of enzymatic reductive amination with formate dehydrogenase-based in situ-cofactor
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

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