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Merck
모든 사진(2)

주요 문서

F8649

Sigma-Aldrich

Formate Dehydrogenase from Candida boidinii

lyophilized powder, 5.0-15.0 units/mg protein

동의어(들):

FDH, Formate:NAD+ oxidoreductase

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About This Item

CAS Number:
효소 위원회 번호:
EC Number:
MDL number:
UNSPSC 코드:
12352204
NACRES:
NA.54

생물학적 소스

fungus (Candida boidinii)

Quality Level

양식

lyophilized powder

특이 활성도

5.0-15.0 units/mg protein

구성

Protein, 5.0-20.0% biuret

저장 온도

2-8°C

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애플리케이션

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.

생화학적/생리학적 작용

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.

단위 정의

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.

픽토그램

Health hazard

신호어

Danger

유해 및 위험 성명서

예방조치 성명서

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

개인 보호 장비

Eyeshields, Gloves, type N95 (US)


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문서 라이브러리 방문

이미 열람한 고객

Held in police custody.
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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)
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
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
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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