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L9795

Sigma-Aldrich

Lactate Oxidase from Aerococcus viridans

lyophilized powder

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Synonym(s):
L-lactate monooxygenase, lactate monooxygenase, lactate oxidative decarboxylase, lactate oxygenase, lactic oxidase, lactic oxygenase
NACRES:
NA.54

biological source

bacterial (Aerococcus viridans)

Quality Level

200

form

lyophilized powder

mol wt

80 kDa (gel filtration)

storage temp.

−20°C

General description

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

Application

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

Biochem/physiol Actions

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.

Unit Definition

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.

Pictograms

Exclamation markHealth hazard
GHS07,GHS08

Signal Word

Danger

Hazard Statements

H315 - H319 - H334 - H335

Hazard Classifications

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

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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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
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;
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
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
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