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Key Documents

L9795

Sigma-Aldrich

Lactate Oxidase from Aerococcus viridans

lyophilized powder

Synonyme(s) :

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

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About This Item

Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

bacterial (Aerococcus viridans)

Niveau de qualité

Forme

lyophilized powder

Poids mol.

80 kDa (gel filtration)

Température de stockage

−20°C

Description générale

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

Actions biochimiques/physiologiques

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.

Définition de l'unité

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.

Pictogrammes

Health hazardExclamation mark

Mention d'avertissement

Danger

Mentions de danger

Classification des risques

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

Organes cibles

Respiratory system

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

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
Yashwanth Ashok et al.
PloS one, 15(2), e0223870-e0223870 (2020-02-25)
Lactate oxidases belong to a group of FMN-dependent enzymes and they catalyze a conversion of lactate to pyruvate with a release of hydrogen peroxide. Hydrogen peroxide is also utilized as a read out in biosensors to quantitate lactate levels in
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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