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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
Sabrina Witthoff et al.
Microbiology (Reading, England), 158(Pt 9), 2428-2439 (2012-07-07)
Here, we show that Corynebacterium glutamicum ATCC 13032 co-metabolizes formate when it is grown with glucose as the carbon and energy source. CO(2) measurements during bioreactor cultivation and use of (13)C-labelled formate demonstrated that formate is almost completely oxidized to
Matteo Tiberti et al.
Inorganic chemistry, 51(15), 8331-8339 (2012-07-18)
DFT/BP86/TZVP and DFT/B3LYP/TZVP have been used to investigate systematically the reaction pathways associated with the H-transfer step, which is the rate-determining step of the reaction HCOO(-) ⇄ CO(2) + H(+) + 2e(-), as catalyzed by metalloenzyme formate dehydrogenase (FDH). Actually

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