L9795
Lactate Oxidase from Aerococcus viridans
lyophilized powder
Sinónimos:
L-lactate monooxygenase, lactate monooxygenase, lactate oxidative decarboxylase, lactate oxygenase, lactic oxidase, lactic oxygenase
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About This Item
NACRES:
NA.54
UNSPSC Code:
12352204
Nombre del producto
Lactate Oxidase from Aerococcus viridans, lyophilized powder
Quality Level
biological source
bacterial (Aerococcus viridans)
form
lyophilized powder
mol wt
80 kDa (gel filtration)
storage temp.
−20°C
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.
General description
Lactate oxidase (LOX) is a flavin mononucleotide (FMN)-dependent enzyme and is a member of the α-hydroxy-acid oxidase flavoenzyme family.
Other Notes
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.
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Clase de almacenamiento
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_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
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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