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F8649

Sigma-Aldrich

Formate Dehydrogenase from Candida boidinii

lyophilized powder, 5.0-15.0 units/mg protein

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
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
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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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)
Held in police custody.
A Skelt
Nursing times, 84(4), 50-52 (1988-01-02)
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
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
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
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