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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Acerca de este artículo
NACRES:
NA.54
UNSPSC Code:
12352204
Biological source:
bacterial (Aerococcus viridans)
Servicio técnico
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Permítanos ayudarleQuality Level
biological source
bacterial (Aerococcus viridans)
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.
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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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;
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
Tania Pomili et al.
Biosensors, 11(11) (2021-11-26)
In this study, we describe a monolithic and fully integrated paper-based device for the simultaneous detection of three prognostic biomarkers in saliva. The pattern of the proposed multiplexed device is designed with a central sample deposition zone and three identical
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