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Information on EC 1.1.3.2 - L-lactate oxidase
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1.1.3.2 L-lactate oxidaseIUBMB Comments
Contains flavin mononucleotide (FMN). The best characterized enzyme is that from the bacterium Aerococcus viridans. The enzyme is widely used in biosensors to measure the lactate concentration in blood and other tissues.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
l-lactate oxidase, avlox, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-lactate oxidase
LctO
LOX
LctO
-
-
-
-
LOX
-
-
ambiguous
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-lactate + O2 = pyruvate + H2O2
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
(S)-lactate:oxygen 2-oxidoreductase
Contains flavin mononucleotide (FMN). The best characterized enzyme is that from the bacterium Aerococcus viridans. The enzyme is widely used in biosensors to measure the lactate concentration in blood and other tissues.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-hydroxy-2-(4-chlorophenyl)acetate + O2
(4-chlorophenyl)pyruvate + H2O2
-
-
-
?
2-hydroxy-2-(4-hydroxyphenyl)acetate + O2
(4-hydroxyphenyl)pyruvate + H2O2
-
-
-
?
2-hydroxy-2-(4-methoxyphenyl)acetate + O2
(4-methoxyphenyl)pyruvate + H2O2
-
-
-
?
2-hydroxy-2-(4-methylphenyl)acetate + O2
(4-methylphenyl)pyruvate + H2O2
-
-
-
?
2-hydroxy-2-(4-nitrophenyl)acetate + O2
(4-nitrophenyl)pyruvate + H2O2
-
-
-
?
glyoxylate + O2
oxalate + H2O2
15.3% of the activity with L-lactate
-
-
?
L-alpha-hydroxy-beta-methylvalerate + O2
3-methyl-2-oxopentanoate + H2O2
-
-
-
?
L-malic acid + 2,6-dichlorophenolindophenol
?
Gram-negative soil bacterium
-
no decarboxylation
-
-
?
(R)-lactate + 2,6-dichlorophenolindophenol
?
Gram-negative soil bacterium
-
no decarboxylation
-
-
?
(R)-lactate + 2,6-dichlorophenolindophenol
?
Gram-negative soil bacterium KY6
-
no decarboxylation
-
-
?
(S)-lactate + 2,6-dichlorophenolindophenol
pyruvate + ?
Gram-negative soil bacterium
-
no decarboxylation
-
-
?
(S)-lactate + 2,6-dichlorophenolindophenol
pyruvate + ?
Gram-negative soil bacterium KY6
-
no decarboxylation
-
-
?
(S)-lactate + O2
pyruvate + H2O2
-
-
-
?
(S)-lactate + O2
pyruvate + H2O2
-
strict specificity to L-lactate. The enzyme does not oxidize fumarate, pyruvate, succinate, ascorbate, dihydroxyacetone, glycolate, D-lactate, D,L-2-hydroxybutyrate and D,L-alanine or D-serine
-
-
?
(S)-lactate + O2
pyruvate + H2O2
-
strict specificity to L-lactate. The enzyme does not oxidize fumarate, pyruvate, succinate, ascorbate, dihydroxyacetone, glycolate, D-lactate, D,L-2-hydroxybutyrate and D,L-alanine or D-serine
-
-
?
(S)-lactate + O2
pyruvate + H2O2
-
strict specificity to L-lactate. The enzyme does not oxidize fumarate, pyruvate, succinate, ascorbate, dihydroxyacetone, glycolate, D-lactate, D,L-2-hydroxybutyrate and D,L-alanine or D-serine
-
-
?
(S)-lactate + O2
pyruvate + H2O2
-
strict specificity to L-lactate. The enzyme does not oxidize fumarate, pyruvate, succinate, ascorbate, dihydroxyacetone, glycolate, D-lactate, D,L-2-hydroxybutyrate and D,L-alanine or D-serine
-
-
?
(S)-lactate + O2
pyruvate + H2O2
-
strict specificity to L-lactate. The enzyme does not oxidize fumarate, pyruvate, succinate, ascorbate, dihydroxyacetone, glycolate, D-lactate, D,L-2-hydroxybutyrate and D,L-alanine or D-serine
-
-
?
(S)-lactate + O2
pyruvate + H2O2
-
strict specificity to L-lactate. The enzyme does not oxidize fumarate, pyruvate, succinate, ascorbate, dihydroxyacetone, glycolate, D-lactate, D,L-2-hydroxybutyrate and D,L-alanine or D-serine
-
-
?
(S)-lactate + O2
pyruvate + H2O2
-
strict specificity to L-lactate. The enzyme does not oxidize fumarate, pyruvate, succinate, ascorbate, dihydroxyacetone, glycolate, D-lactate, D,L-2-hydroxybutyrate and D,L-alanine or D-serine
-
-
?
(S)-lactate + O2
pyruvate + H2O2
-
strict specificity to L-lactate. The enzyme does not oxidize fumarate, pyruvate, succinate, ascorbate, dihydroxyacetone, glycolate, D-lactate, D,L-2-hydroxybutyrate and D,L-alanine or D-serine
-
-
?
(S)-lactate + O2
pyruvate + H2O2
Yarrowia lipolytica VKM Y-2373
-
strict specificity to L-lactate. The enzyme does not oxidize fumarate, pyruvate, succinate, ascorbate, dihydroxyacetone, glycolate, D-lactate, D,L-2-hydroxybutyrate and D,L-alanine or D-serine
-
-
?
(S)-lactate + O2
pyruvate + H2O2
Yarrowia lipolytica VKM Y-2378
-
strict specificity to L-lactate. The enzyme does not oxidize fumarate, pyruvate, succinate, ascorbate, dihydroxyacetone, glycolate, D-lactate, D,L-2-hydroxybutyrate and D,L-alanine or D-serine
-
-
?
(S)-lactate + O2
pyruvate + H2O2
Yarrowia lipolytica VKM Y-47
-
strict specificity to L-lactate. The enzyme does not oxidize fumarate, pyruvate, succinate, ascorbate, dihydroxyacetone, glycolate, D-lactate, D,L-2-hydroxybutyrate and D,L-alanine or D-serine
-
-
?
glycerate + O2
hydroxypyruvate + H2O2
5.9% of the activity with L-lactate
-
-
?
glycolate + 2,6-dichlorophenolindophenol
?
Gram-negative soil bacterium
-
no decarboxylation
-
-
?
glycolate + 2,6-dichlorophenolindophenol
?
Gram-negative soil bacterium KY6
-
no decarboxylation
-
-
?
L-2-hydroxyisocaproate + 2,6-dichlorophenolindophenol
?
Gram-negative soil bacterium
-
no decarboxylation
-
-
?
L-2-hydroxyisocaproate + 2,6-dichlorophenolindophenol
?
Gram-negative soil bacterium KY6
-
no decarboxylation
-
-
?
lactate + 2,6-dichlorophenolindophenol
?
Gram-negative soil bacterium
-
no decarboxylation
-
-
?
lactate + 2,6-dichlorophenolindophenol
?
Gram-negative soil bacterium KY6
-
no decarboxylation
-
-
?
additional information
?
-
a two-step equilibrium precedes the chemical reaction step, in which the second equilibrium step provides an upper limit to the rate with which the particular substrate or ligand is positioned with the flavin in the correct fashion. Results indicate development of significant negative charge in the transition states of the reactions. For reduction by substrate, the results are consistent either with a hydride transfer mechanism or with the carbanion mechanism, in which the substrate alpha-proton is abstracted by an enzyme base protected from exchange with solvent
-
-
?
additional information
?
-
-
a two-step equilibrium precedes the chemical reaction step, in which the second equilibrium step provides an upper limit to the rate with which the particular substrate or ligand is positioned with the flavin in the correct fashion. Results indicate development of significant negative charge in the transition states of the reactions. For reduction by substrate, the results are consistent either with a hydride transfer mechanism or with the carbanion mechanism, in which the substrate alpha-proton is abstracted by an enzyme base protected from exchange with solvent
-
-
?
additional information
?
-
contrary to lactate monooxygenase, with lactate oxidase the complex of reduced flavin enzyme and pyruvate dissociates rapidly, with the result that it is the free reduced flavin form of the enzyme that reacts with O2, to give the observed products, pyruvate and H2O2
-
-
?
additional information
?
-
-
contrary to lactate monooxygenase, with lactate oxidase the complex of reduced flavin enzyme and pyruvate dissociates rapidly, with the result that it is the free reduced flavin form of the enzyme that reacts with O2, to give the observed products, pyruvate and H2O2
-
-
?
additional information
?
-
enzyme is highly specific for L-lactate. No substrates: D-lactate, glycolate and DL-2-hydroxybutanoate
-
-
?
additional information
?
-
mechanism with little development of charge in the transition state, such as a transfer of hydride to the flavin N(5) position or a synchronous mechanism in which the alpha-C-H is formally abstracted as a H+ while the resulting charge is simultaneously neutralized by another event
-
-
?
additional information
?
-
redox potential difference is a dominant factor in determing rate of reduction. The enzyme reconstituted with a series of flavins modified at 6 or 8 position of the isoalloxazine ring shows a close linear relationship between reduction rate constant and redox potential in the ranges of -250 mV to -100 mV when L-lactate is used as substrate. The reconstituted enzyme shows a close linear relationship in the ranges of -150 mV to +100 mV when L-mandelate is used as substrate
-
-
?
additional information
?
-
no substrate: D-lactate. Poor substrate: glycolate
-
-
?
additional information
?
-
-
no substrate: D-lactate. Poor substrate: glycolate
-
-
?
additional information
?
-
no substrate: D-lactate. Poor substrate: glycolate
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FMN
flavin reduction is a direct measure of alpha-C-H bond breakage
FMN
FMN is positioned deep down in the funnel-shaped substrate-binding site, behind (or underneath) the substrate when it is bound. Residues Tyr40, Pro93, Gln144, Tyr146, Thr172, Lys241, Asp296, Arg300 and Arg320 are involved in binding
FMN
removal of FMN and reconstitution of the apoprotein with 12 FMN derivatives with various substituents at the flavin 6- and 8-positions show an increase in the reduction rate constant with increasing redox potential, except that, with lactate, a limiting rate constant is obtained with flavins of high potential
FMN
The standard redox potentials of enzyme-FMN/enzyme-FMNH and enzyme-FMNH/enzyme-FMNH2 are -95 mV and -161 mV, respectively, at pH 7.0, 25°C in 0.01 M imidazol buffer
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cibacron blue 3GA
at low concentrations, Cibacron Blue 3GA behaves as a dye-, pH- and time-dependent inhibitor, non-linear inhibition
Lactate
growth rates of Streptococcus iniae expressing the type 2 enzyme are not reduced at lactate concentrations of 0.3% and 0.5%, whereas a strain expressing the type 1 enzyme exhibits reduced growth rates at these lactate concentrations
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
detailed analysis of reductive and oxidative half-reaction
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cf. EC 1.1.3.1, enzyme shows high L-lactate oxidase and low glycolate oxidase activities
UniProt
brenda
cf. EC 1.1.3.1, enzyme shows high L-lactate oxidase and low glycolate oxidase activities
UniProt
brenda
-
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
intermembrane space. H2O2 is produced independently on the respiratory chain with 1:1 stoichiometry with pyruvate, due to a putative flavin-dependent L-lactate oxidase restricted to the intermembrane space
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
L-lactategrown cells and cells grown on glucose and adapted to various stress conditions are similar, with increased mitochondria, elevated number and size of peroxisomes, and formation of lipid and polyphosphate inclusions
physiological function
overexpression decreases the accumulation of toxic glycolate in a cyanobacterial photorespiratory mutant and restores its ability to grow in air. A lactate oxidase-deficient Nostoc sp. mutant grows normally in nitrate-containing medium but dies under N2-fixing conditions. The enzyme may primarily serve as an O2-scavenging enzyme to protect nitrogenase in extant N2-fixing cyanobacteria
physiological function
Yarrowia lipolytica VKM Y-2378
-
L-lactategrown cells and cells grown on glucose and adapted to various stress conditions are similar, with increased mitochondria, elevated number and size of peroxisomes, and formation of lipid and polyphosphate inclusions
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). D4YFM2_AERVM
Aerococcus viridans (strain ATCC 11563 / DSM 20340 / CCUG 4311 / JCM 20461 / NBRC 12219 / NCTC 8251 / M1)
374
0
40862
TrEMBL
-
LOX_AERVM
Aerococcus viridans (strain ATCC 11563 / DSM 20340 / CCUG 4311 / JCM 20461 / NBRC 12219 / NCTC 8251 / M1)
374
0
40933
Swiss-Prot
-
LOX_NOSS1
Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
365
0
39165
Swiss-Prot
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
?
Gram-negative soil bacterium KY6
-
? * 45000, SDS-PAGE
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
1.9 A crystal structure, Y191F variant bound with FMN and pyruvate. Mutation has a strictly locally disruptive effect
in complex with pyruvate, to 1.9 A resolution. One pyruvate molecule binds to the active site and locates near the N5 position of FMN for subunits, A, B, and D in the asymmetric unit. The pyruvate molecule is stabilized by the interaction of its carboxylate group with the side-chain atoms of Tyr40, Arg181, His265, and Arg268, and of its keto-oxygen atom with the side-chain atoms of Tyr146, Tyr215, and His265
mutant A95G in complex with pyruvate, to 1.65 A resolution. Mutation leads to increased steric volume available in the active site
mutant Y215F in complex with pyruvate, to 2.6 A resolution. The hydrogen bond between the phenolic hydroxyl and the keto oxygen in pyruvate is replaced with a potentially stronger hydrophobic interaction between the phenylalanine and the methyl group of pyruvate. Residues 200 through 215 or 216 appear to be disordered
native enzyme and its complex with D-lactate at pH 4.5. In the complex structure, the D-lactate resides in the substrate-binding site, but acitve site His265 flips far away from the D-lactate, as compared with its conformation in the unbound state at pH 8.0. The flip of His265 triggers a large structural rearrangement. The reductive half-reaction mechanism may release pyruvate through hydride transfer. In the oxidative half-reaction, His265 flips back, pushing molecular oxygen into the substrate-binding site as the second substrate, and the reverse reaction takes place to produce hydrogen peroxide
to 2.1 A resolution. LOX crystallizes as two tightly packed tetramers in the asymmetric unit, each having fourfold symmetry. Residues Tyr40, Arg268, His265, Tyr146 and Asp174 are involved in substrate binding
to 2.1 A resolution. The LOX monomer structure has a typical alpha8/beta8 motif. Five residues around the FMN prosthetic group of LOX, act synergistically to discriminate between the L/D configurations of lactate. Space group I422 with unit-cell parameters a = b = 191.096 A , c = 194.497A and a = b = c = 90 with four monomers per asymmetric unit
to 3.0 A resolution, space group P212121 with unit cell parameters a = 118.4 A, b = 138.4 A, c = 104.6 A. The enzyme may exist as an octameric form with noncrystallographic two- and four-fold axes in the center of the octamer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A95G
A96L
A96L/N212K
the double mutant shows a drastic decrease compared with that of the wild type (0.16% using 20 mM L-lactate) and A96L mutant (1.9% using 20 mM L-lactate). The mutant enzyme is more stable than the wild type enzyme and the N212K single mutant. After modification by phenazine ethosulfate, the Ala96Leu/Asn212Lys double mutant shows the highest oxidation peak in the presence of L-lactate, whereas the electrodes with the phenazine ethosulfate-modified wild type or Ala96Leu mutant do not
R181K
mutation in conserved residue, efficiency of reduction of the oxidized flavin by L-lactate is greatly reduced
R181K/R268K
mutation in conserved residue, efficiency of reduction of the oxidized flavin by L-lactate is greatly reduced
R181M
mutation in conserved residue, efficiency of reduction of the oxidized flavin by L-lactate is greatly reduced
R268K
mutation in conserved residue, efficiency of reduction of the oxidized flavin by L-lactate is greatly reduced. Mutation also results in a slow conversion of the 8-CH3-substituent of FMN to yield 8-formyl-FMN
S218C
introduction of a site for chemical modification, about 50% of wild-type activity
Y191A
28fold decrease in release of pyruvate, , binding of L-lactate is strongly affected
Y191L
19fold decrease in release of pyruvate, binding of L-lactate is strongly affected
Y215F
mutation in binding pocket, mutant shows slowed flavin reduction and oxidation by up to 33-fold. Pyruvate release is also decelerated and is the slowest step overall
Y215H Y215F
mutation in binding pocket, mutant shows slowed flavin reduction and oxidation by up to 33-fold. Pyruvate release is also decelerated
A96L
-
the mutant enzyme is more stable than the wild type enzyme and the N212K single mutant
-
A96L/N212K
-
the double mutant shows a drastic decrease compared with that of the wild type (0.16% using 20 mM L-lactate) and A96L mutant (1.9% using 20 mM L-lactate). The mutant enzyme is more stable than the wild type enzyme and the N212K single mutant. After modification by phenazine ethosulfate, the Ala96Leu/Asn212Lys double mutant shows the highest oxidation peak in the presence of L-lactate, whereas the electrodes with the phenazine ethosulfate-modified wild type or Ala96Leu mutant do not
-
F212V
change in the active site to that of Arabidopsis thaliana glycolate oxidase 2, 25fold decrease in the L-lactate oxidase/glycolate oxidase activity ratio
L112W
change in the active site to that of Arabidopsis thaliana glycolate oxidase 2, 2fold decrease in the L-lactate oxidase/glycolate oxidase activity ratio
M82T
change in the active site to that of Arabidopsis thaliana glycolate oxidase 2, 10fold decrease in the L-lactate oxidase/glycolate oxidase activity ratio
M82T/L112W/F212V
change in the active site to that of Arabidopsis thaliana glycolate oxidase 2, reverse the L-lactate oxidase/glycolate oxidase activity ratio
additional information
gene variant type 2 reveals a 51-nucleotide insertion in LctO, resulting in a 17-amino-acid repeat in the gene product, and formation of an extra loop in the monomeric protein structure. Upon expression in Escherichia coli, the higher-molecular-weight type 2 enzyme exhibits higher activity. Growth rates of Streptococcus iniae expressing the type 2 enzyme are not reduced at lactate concentrations of 0.3% and 0.5%, whereas a strain expressing the type 1 enzyme exhibits reduced growth rates at these lactate concentrations
A95G
activity with L-lactate similar to wild-type, increased activity with longer chain L-alpha-hydroxyacids such as alpha-hydroxy-n-butyric acid, alpha-hydroxy-n-valeric acid, and also with L-mandelic acid. Reduction of the enzyme bound flavin by substrates is the rate-limiting step in A95G
A95G
mutant is 3fold more reactive towards 2,6-dichlorophenol-indophenol than O2, whereas wildtype is 14fold more reactive towards O2 than 2,6-dichlorophenol-indophenol. Substituted 1,4-benzoquinones are up to 5fold better electron acceptors for reaction with L-lactate-reduced A95G variant than wild-type
A96L
engineering the enzyme in order to minimize the effects of oxygen interference on sensor strips. Mutant A96L shows a drastic reduction in oxidase activity using molecular oxygen as the electron acceptor and a small increase in dehydrogenase activity employing an artificial electron acceptor. After immobilization on a screen-printed carbon electrode and under argon or atmospheric conditions, the response current increases linearly from 0.05 to 0.5 mM L-lactate for both wild-type and mutant A96L. Under atmospheric conditions, the response of wild-type electrode is suppressed by 9-12% due to oxygen interference. The mutant maintains 56-69% of the response current at the same L-lactate level and minimizes the relative bias error to -19% from -49% of wild-type
A96L
the mutant enzyme is more stable than the wild type enzyme and the N212K single mutant
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.7 - 9.5
Gram-negative soil bacterium
-
stable for 24 h at 4°C
440395
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is induced during growth on L-lactate in the exponential growth phase and by growth on glucose after adaptation to stress conditions
expression is induced during growth on L-lactate in the exponential growth phase and by growth on glucose after adaptation to stress conditions
-
expression is induced during growth on L-lactate in the exponential growth phase and by growth on glucose after adaptation to stress conditions
Yarrowia lipolytica VKM Y-2378
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
biotechnology
coupling of mutant S218C in 94% yield to maleimide-activated methoxypoly(ethylene glycol) 5000. PEGylation causes about 30% small decrease in the specific activity of the S218C mutant, and it does not change the protein stability
diagnostics
food industry
medicine
synthesis
analysis
-
development of a bienzyme fiberoptic sensor for flow injection analysis of L-lactate using lactate oxidase and peroxidase immobilized on a polyamide membrane. Hydrogen peroxide generated by lactate oxidase is substrate of peroxidase in presence of luminol. For the sensor strip, the detection limit is 250 pmol lactate, with 1.7% variation for 10 replicates using 6.25 nmol lactate
analysis
engineering the enzyme in order to minimize the effects of oxygen interference on sensor strips. Mutant A96L shows a drastic reduction in oxidase activity using molecular oxygen as the electron acceptor and a small increase in dehydrogenase activity employing an artificial electron acceptor. After immobilization on a screen-printed carbon electrode and under argon or atmospheric conditions, the response current increases linearly from 0.05 to 0.5 mM L-lactate for both wild-type and mutant A96L. Under atmospheric conditions, the response of wild-type electrode is suppressed by 9-12% due to oxygen interference. The mutant maintains 56-69% of the response current at the same L-lactate level and minimizes the relative bias error to -19% from -49% of wild-type
diagnostics
-
an improved amperometric L-lactate biosensor was constructed based on covalent immobilization of lactate oxidase from Pediococcus species onto carboxylated multiwalled carbon nanotubes (cMWCNT)/copper nanoparticles (CuNPs)/polyaniline (PANI) hybrid film electrodeposited on the surface of a pencil graphite electrode. The biosensor shows maximum response within 5 s at pH 8.0 in 0.05 M sodium phosphate buffer and 37°C, when operated at 20 mV/s. The biosensor has a detection limit of 0.00025 mM with a wide working range between 0.001-2.5 mM. The biosensor is employed for measurement of L-lactic acid level in plasma of apparently healthy and diseased persons. Analytical recovery of added lactic acid in plasma is 95.5%. The working enzyme electrode is used 180 times over a period of 140 days, when stored at 4°C
diagnostics
-
an integrated tear lactate sensor using Schirmer test strip and engineered lactate oxidase is developed. The sensor is insensitive to ascorbic acid, acetaminophen, and uric acid, which are common interfering compounds in tears, and show no sign of degradation after 8 weeks of shelf life study. The proposed sensor exhibits potential usefulness in providing an alternative noninvasive method of measuring lactate and in calibrating the continuous lactate contact lens
diagnostics
L-lactate oxidase based lactate sensors are widely used for clinical diagnostics, sports medicine, and food quality control. Rational engineering of Aerococcus viridans L-lactate oxidase for the mediator modification to achieve quasi-direct electron transfer type lactate sensor
diagnostics
-
L-lactate oxidase based lactate sensors are widely used for clinical diagnostics, sports medicine, and food quality control. Rational engineering of Aerococcus viridans L-lactate oxidase for the mediator modification to achieve quasi-direct electron transfer type lactate sensor
-
food industry
L-lactate oxidase based lactate sensors are widely used for clinical diagnostics, sports medicine, and food quality control. Rational engineering of Aerococcus viridans L-lactate oxidase for the mediator modification to achieve quasi-direct electron transfer type lactate sensor
food industry
-
L-lactate oxidase based lactate sensors are widely used for clinical diagnostics, sports medicine, and food quality control. Rational engineering of Aerococcus viridans L-lactate oxidase for the mediator modification to achieve quasi-direct electron transfer type lactate sensor
-
medicine
L-lactate oxidase based lactate sensors are widely used for clinical diagnostics, sports medicine, and food quality control. Rational engineering of Aerococcus viridans L-lactate oxidase for the mediator modification to achieve quasi-direct electron transfer type lactate sensor
medicine
-
L-lactate oxidase based lactate sensors are widely used for clinical diagnostics, sports medicine, and food quality control. Rational engineering of Aerococcus viridans L-lactate oxidase for the mediator modification to achieve quasi-direct electron transfer type lactate sensor
-
synthesis
biocascade synthesis of L-tyrosine derivatives by coupling a thermophilic tyrosine phenol-lyase and L-lactate oxidase. o-Phenol derivatives are transformed into the corresponding L-tyrosine derivatives with excellent stereoselectivity and high yields using an efficient one-pot, two-step cascade containing thermophilic tyrosine phenol-lyase mutants from Symbiobacterium toebii and L-lactate oxidase from Aerococcus viridans
synthesis
-
enzymatic preparation of pyruvate by a whole-cell biocatalyst coexpressing L-lactate oxidase and catalase. Under the optimized transformation conditions, pyruvate is produced at a titer of 59.9 g/l and a yield of 90.8% in a substrate fed-batch process, promising an alternative route for the green production of pyruvate
synthesis
-
biocascade synthesis of L-tyrosine derivatives by coupling a thermophilic tyrosine phenol-lyase and L-lactate oxidase. o-Phenol derivatives are transformed into the corresponding L-tyrosine derivatives with excellent stereoselectivity and high yields using an efficient one-pot, two-step cascade containing thermophilic tyrosine phenol-lyase mutants from Symbiobacterium toebii and L-lactate oxidase from Aerococcus viridans
-
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REF.
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TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Xu, P.; Yano, T.; Yamamoto, K.; Suzuki, H.; Kumagai, H.
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Aerococcus viridans (Q44467), Aerococcus viridans
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Crystallographic study on the interaction of L-lactate oxidase with pyruvate at 1.9 Angstrom resolution
Biochem. Biophys. Res. Commun.
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Aerococcus viridans (Q44467), Aerococcus viridans
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Maeda-Yorita, K.; Aki, K.; Sagai, H.; Misaki, H.; Massey, V.
L-lactate oxidase and L-lactate monooxygenase mechanistic variations on a common structural theme
Biochimie
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1995
Aerococcus viridans (Q44467), Aerococcus viridans
brenda
Morimoto, Y.; Yorita, K.; Aki, K.; Misaki, H.; Massey, V.
L-lactate oxidase from Aerococcus viridans crystallized as an octamer. Preliminary X-ray studies
Biochimie
80
309-312
1998
Aerococcus viridans (Q44467), Aerococcus viridans
brenda
Unterweger, B.; Stoisser, T.; Leitgeb, S.; Birner-Gruenberger, R.; Nidetzky, B.
Engineering of Aerococcus viridans L-lactate oxidase for site-specific PEGylation characterization and selective bioorthogonal modification of a S218C mutant
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23
1406-1414
2012
Aerococcus viridans (Q44467), Aerococcus viridans
brenda
Aki, K.; Yorita, K.; Massey, V.
Thermodynamic properties of L-lactate oxidase reconstituted with modified flavins
Biofactors
11
115-116
2000
Aerococcus viridans (Q44467)
brenda
Hiraka, K.; Kojima, K.; Lin, C.E.; Tsugawa, W.; Asano, R.; La Belle, J.T.; Sode, K.
Minimizing the effects of oxygen interference on l-lactate sensors by a single amino acid mutation in Aerococcus viridans L-lactate oxidase
Biosens. Bioelectron.
103
163-170
2018
Aerococcus viridans (Q44467), Aerococcus viridans
brenda
Berger, A.; Blum, L.
Enhancement of the response of a lactate oxidase/peroxidase-based fiberoptic sensor by compartmentalization of the enzyme layer
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16
979-984
1994
Pediococcus sp.
-
brenda
Stoisser, T.; Klimacek, M.; Wilson, D.K.; Nidetzky, B.
Speeding up the product release a second-sphere contribution from Tyr191 to the reactivity of L-lactate oxidase revealed in crystallographic and kinetic studies of site-directed variants
FEBS J.
282
4130-4140
2015
Aerococcus viridans (Q44467), Aerococcus viridans
brenda
Stoisser, T.; Rainer, D.; Leitgeb, S.; Wilson, D.K.; Nidetzky, B.
The Ala95-to-Gly substitution in Aerococcus viridans l-lactate oxidase revisited - structural consequences at the catalytic site and effect on reactivity with O2 and other electron acceptors
FEBS J.
282
562-578
2015
Aerococcus viridans (Q44467)
brenda
de Bari, L.; Valenti, D.; Atlante, A.; Passarella, S.
L-lactate generates hydrogen peroxide in purified rat liver mitochondria due to the putative L-lactate oxidase localized in the intermembrane space
FEBS Lett.
584
2285-2290
2010
Rattus norvegicus
brenda
Yorita, K.; Aki, K.; Ohkuma-Soyejima, T.; Kokubo, T.; Misaki, H.; Massey, V.
Conversion of L-lactate oxidase to a long chain alpha-hydroxyacid oxidase by site-directed mutagenesis of alanine 95 to glycine
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271
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1996
Aerococcus viridans (Q44467), Aerococcus viridans
brenda
Streitenberger, S.A.; Lopez-Mas, J.A.; Sanchez-Ferrer, A.; Garcia-Carmona, F.
Non-linear slow-binding inhibition of Aerococcus viridans lactate oxidase by Cibacron Blue 3GA
J. Enzyme Inhib.
16
301-312
2001
Aerococcus viridans (D4YFM2), Aerococcus viridans ATCC 11563 (D4YFM2)
brenda
Furuichi, M.; Suzuki, N.; Dhakshnamoorhty, B.; Minagawa, H.; Yamagishi, R.; Watanabe, Y.; Goto, Y.; Kaneko, H.; Yoshida, Y.; Yagi, H.; Waga, I.; Kumar, P.K.; Mizuno, H.
X-ray structures of Aerococcus viridans lactate oxidase and its complex with D-lactate at pH 4.5 show an alpha-hydroxyacid oxidation mechanism
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378
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Aerococcus viridans (Q44467), Aerococcus viridans
brenda
Arinbasarova, A.; Biryukova, E.; Suzina, N.; Medentsev, A.
Synthesis and localization of L-lactate oxidase in yeasts Yarrowia lipolytica
Microbiology
83
505-509
2014
Yarrowia lipolytica, Yarrowia lipolytica VKM Y-2378
-
brenda
Hackenberg, C.; Kern, R.; Huege, J.; Stal, L.J.; Tsuji, Y.; Kopka, J.; Shiraiwa, Y.; Bauwe, H.; Hagemann, M.
Cyanobacterial lactate oxidases serve as essential partners in N2 fixation and evolved into photorespiratory glycolate oxidases in plants
Plant Cell
23
2978-2990
2011
Chlamydomonas reinhardtii (F8WQN2), Chlamydomonas reinhardtii, Nostoc sp. PCC 7120 = FACHB-418 (Q8Z0C8)
brenda
Yorita, K.; Janko, K.; Aki, K.; Ghisla, S.; Palfey, B.A.; Massey, V.
On the reaction mechanism of L-lactate oxidase quantitative structure-activity analysis of the reaction with para-substituted L-mandelates
Proc. Natl. Acad. Sci. USA
94
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1997
Aerococcus viridans (Q44467)
brenda
Yorita, K.; Matsuoka, T.; Misaki, H.; Massey, V.
Interaction of two arginine residues in lactate oxidase with the enzyme flavin conversion of FMN to 8-formyl-FMN
Proc. Natl. Acad. Sci. USA
97
13039-13044
2000
Aerococcus viridans (Q44467)
brenda
Yorita, K.; Misaki, H.; Palfey, B.A.; Massey, V.
On the interpretation of quantitative structure-function activity relationship data for lactate oxidase
Proc. Natl. Acad. Sci. USA
97
2480-2485
2000
Aerococcus viridans (Q44467), Aerococcus viridans
brenda
Stoisser, T.; Brunsteiner, M.; Wilson, D.K.; Nidetzky, B.
Conformational flexibility related to enzyme activity evidence for a dynamic active-site gatekeeper function of Tyr(215) in Aerococcus viridans lactate oxidase
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6
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2016
Aerococcus viridans (Q44467), Aerococcus viridans
brenda
Biryukova, E.; Arinbasarova, A.; Medentsev, A.
Synthesis of L-lactate oxidaze in yeast Yarrowia lipolytica during submerged cultivation
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53
217-221
2017
Yarrowia lipolytica, Yarrowia lipolytica VKM Y-47, Yarrowia lipolytica VKM Y-2378, Yarrowia lipolytica VKM Y-2373, Yarrowia lipolytica 655, Yarrowia lipolytica 672, Yarrowia lipolytica 667, Yarrowia lipolytica 668, Yarrowia lipolytica 585, Yarrowia lipolytica 645, Yarrowia lipolytica 646
brenda
Hiraka, K.; Kojima, K.; Tsugawa, W.; Asano, R.; Ikebukuro, K.; Sode, K.
Rational engineering of Aerococcus viridansl-lactate oxidase for the mediator modification to achieve quasi-direct electron transfer type lactate sensor
Biosens. Bioelectron.
151
111974
2020
Aerococcus viridans (D4YFM2), Aerococcus viridans, Aerococcus viridans ATCC 11563 (D4YFM2)
brenda
Dagar, K.; Pundir, C.
An improved amperometric L-lactate biosensor based on covalent immobilization of microbial lactate oxidase onto carboxylated multiwalled carbon nanotubes/copper nanoparticles/polyaniline modified pencil graphite electrode
Enzyme Microb. Technol.
96
177-186
2017
Pediococcus sp.
brenda
Li, G.; Lian, J.; Xue, H.; Jiang, Y.; Ju, S.; Wu, M.; Lin, J.; Yang, L.
Biocascade synthesis of L-tyrosine derivatives by coupling a thermophilic tyrosine phenol-lyase and L-lactate oxidase
Eur. J. Org. Chem.
2020
1050-1054
2020
Aerococcus viridans (D4YFM2), Aerococcus viridans ATCC 11563 (D4YFM2)
-
brenda
Li, G.; Lian, J.; Xue, H.; Jiang, Y.; Wu, M.; Lin, J.; Yang, L.
Enzymatic preparation of pyruvate by a whole-cell biocatalyst coexpressing L-lactate oxidase and catalase
Process Biochem.
96
113-121
2020
Aerococcus viridans
-
brenda
Lin, C.; Hiraka, K.; Matloff, D.; Johns, J.; Deng, A.; Sode, K.; La Belle, J.
Development toward a novel integrated tear lactate sensor using Schirmer test strip and engineered lactate oxidase
Sens. Actuators B Chem.
270
525-529
2018
Aerococcus viridans
-
brenda
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