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L9795

Sigma-Aldrich

Lactate Oxidase from Aerococcus viridans

lyophilized powder

Sinônimo(s):

L-lactate monooxygenase, lactate monooxygenase, lactate oxidative decarboxylase, lactate oxygenase, lactic oxidase, lactic oxygenase

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About This Item

Código UNSPSC:
12352204
NACRES:
NA.54

fonte biológica

bacterial (Aerococcus viridans)

Nível de qualidade

200

forma

lyophilized powder

peso molecular

80 kDa (gel filtration)

temperatura de armazenamento

−20°C

Descrição geral

Lactate oxidase (LOX) is a flavin mononucleotide (FMN)-dependent enzyme and is a member of the α-hydroxy-acid oxidase flavoenzyme family.

Aplicação

Lactate Oxidase from Aerococcus viridans has been used as a:
  • supplement in the culture medium to convert extracellular lactate to pyruvate
  • coating on glass beads for electrochemical detection of lactate from a single cell by a push-pull nozzle system
  • coating on multi-branched gold nanoparticles (GNPs) for the simultaneous colorimetric detection of lactate in saliva by paper-based multiplexed device

Ações bioquímicas/fisiológicas

Lactate oxidase (LOX) catalyzes the oxidation of lactate to pyruvate and hydrogen peroxide in the presence of an FMN co-factor. The enzyme aids in the determination of L-lactate indirectly by measuring the hydrogen peroxide formed in the reaction.

Definição da unidade

One unit is defined as the amount of enzyme which generates 1m mole of Hydrogen Peroxide per minute at 37°C under standard assay conditions.

Pictogramas

Health hazardExclamation mark
GHS08,GHS07

Palavra indicadora

Danger

Frases de perigo

H315,H319,H334,H335

Classificações de perigo

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Órgãos-alvo

Respiratory system

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

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Nicholas X Williams et al.
Nature electronics, 4(4), 261-268 (2022-04-05)
Electronic waste can lead to the accumulation of environmentally and biologically toxic materials and is a growing global concern. Developments in transient electronics-in which devices are designed to disintegrate after use-have focused on increasing the biocompatibility, whereas efforts to develop
Ingar Leiros et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 62(Pt 12), 1185-1190 (2006-12-05)
The crystal structure of L-lactate oxidase (LOX) from Aerococcus viridans has been determined at 2.1 A resolution. LOX catalyzes the flavin mononucleotide (FMN) dependent oxidation of lactate to pyruvate and hydrogen peroxide. LOX belongs to the alpha-hydroxy-acid oxidase flavoenzyme family;
Lin Zhou et al.
Analytical chemistry, 93(24), 8680-8686 (2021-06-10)
Metabolism of a single cell, even within the same organization, differs from other cells by orders of magnitude. Single-cell analysis provides key information for early diagnosis of cancer as well as drug screening. Any slight change in the microenvironment may
Cyrielle L Bouchez et al.
STAR protocols, 3(2), 101403-101403 (2022-05-24)
Lactate is a central metabolite in energy metabolism and is also involved in cell signaling and epigenetic regulations. Here, we describe an NADH-independent enzymatic assay allowing rapid, selective, and sensitive quantification of L-lactate down to the pmol range. We detail
Melissa Conti Mazza et al.
Journal of neurochemistry, 162(3), 245-261 (2022-06-18)
Human DJ-1 is a cytoprotective protein whose absence causes Parkinson's disease and is also associated with other diseases. DJ-1 has an established role as a redox-regulated protein that defends against oxidative stress and mitochondrial dysfunction. Multiple studies have suggested that
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