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Information on EC 1.1.3.2 - L-lactate oxidase
for references in articles please use BRENDA:EC1.1.3.2
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.3 With oxygen as acceptor
1.1.3.2 L-lactate oxidase
IUBMB 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.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
showSynonyms
l-lactate oxidase, avlox, more
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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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-
-
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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
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-2-hydroxy-2-phenylacetate + O2
phenylpyruvate + H2O2
Substrates: -
Products: -
Products: -
?
(S)-2-hydroxybutanoate + O2
2-oxobutanoate + H2O2
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-(4-chlorophenyl)acetate + O2
(4-chlorophenyl)pyruvate + H2O2
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-(4-hydroxyphenyl)acetate + O2
(4-hydroxyphenyl)pyruvate + H2O2
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-(4-methoxyphenyl)acetate + O2
(4-methoxyphenyl)pyruvate + H2O2
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-(4-methylphenyl)acetate + O2
(4-methylphenyl)pyruvate + H2O2
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-(4-nitrophenyl)acetate + O2
(4-nitrophenyl)pyruvate + H2O2
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-phenylacetate + O2
phenylpyruvate + H2O2
Substrates: -
Products: -
Products: -
?
2-hydroxybutanoate + O2
2-oxobutanoate + H2O2
Substrates: -
Products: -
Products: -
?
2-hydroxypentanoate + O2
2-oxopentanoate + H2O2
Substrates: -
Products: -
Products: -
?
glyoxylate + O2
oxalate + H2O2
Substrates: 15.3% of the activity with L-lactate
Products: -
Products: -
?
L-alpha-hydroxy-beta-methylvalerate + O2
3-methyl-2-oxopentanoate + H2O2
Substrates: -
Products: -
Products: -
?
L-malic acid + 2,6-dichlorophenolindophenol
?
Gram-negative soil bacterium
-
Substrates: no decarboxylation
Products: -
Products: -
?
(R)-lactate + 2,6-dichlorophenolindophenol
?
Gram-negative soil bacterium
-
Substrates: no decarboxylation
Products: -
Products: -
?
(R)-lactate + 2,6-dichlorophenolindophenol
?
Gram-negative soil bacterium KY6
-
Substrates: no decarboxylation
Products: -
Products: -
?
(S)-lactate + 2,6-dichlorophenolindophenol
pyruvate + ?
Gram-negative soil bacterium
-
Substrates: no decarboxylation
Products: -
Products: -
?
(S)-lactate + 2,6-dichlorophenolindophenol
pyruvate + ?
Gram-negative soil bacterium KY6
-
Substrates: no decarboxylation
Products: -
Products: -
?
(S)-lactate + O2
pyruvate + H2O2
Substrates: -
Products: -
Products: -
?
(S)-lactate + O2
pyruvate + H2O2
Substrates: -
Products: -
Products: -
?
(S)-lactate + O2
pyruvate + H2O2
Substrates: -
Products: -
Products: -
?
(S)-lactate + O2
pyruvate + H2O2
Substrates: -
Products: -
Products: -
?
(S)-lactate + O2
pyruvate + H2O2
-
Substrates: 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
Products: -
Products: -
?
(S)-lactate + O2
pyruvate + H2O2
-
Substrates: 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
Products: -
Products: -
?
(S)-lactate + O2
pyruvate + H2O2
-
Substrates: 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
Products: -
Products: -
?
(S)-lactate + O2
pyruvate + H2O2
-
Substrates: 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
Products: -
Products: -
?
(S)-lactate + O2
pyruvate + H2O2
-
Substrates: 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
Products: -
Products: -
?
(S)-lactate + O2
pyruvate + H2O2
-
Substrates: 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
Products: -
Products: -
?
(S)-lactate + O2
pyruvate + H2O2
-
Substrates: 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
Products: -
Products: -
?
(S)-lactate + O2
pyruvate + H2O2
-
Substrates: 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
Products: -
Products: -
?
(S)-lactate + O2
pyruvate + H2O2
Yarrowia lipolytica VKM Y-2373
-
Substrates: 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
Products: -
Products: -
?
(S)-lactate + O2
pyruvate + H2O2
Yarrowia lipolytica VKM Y-2378
-
Substrates: 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
Products: -
Products: -
?
(S)-lactate + O2
pyruvate + H2O2
Yarrowia lipolytica VKM Y-47
-
Substrates: 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
Products: -
Products: -
?
(S)-mandelic acid + O2
phenylpyruvate + H2O2
Substrates: -
Products: -
Products: -
?
(S)-mandelic acid + O2
phenylpyruvate + H2O2
-
Substrates: -
Products: -
Products: -
?
glycerate + O2
hydroxypyruvate + H2O2
Substrates: 5.9% of the activity with L-lactate
Products: -
Products: -
?
glycolate + 2,6-dichlorophenolindophenol
?
Gram-negative soil bacterium
-
Substrates: no decarboxylation
Products: -
Products: -
?
glycolate + 2,6-dichlorophenolindophenol
?
Gram-negative soil bacterium KY6
-
Substrates: no decarboxylation
Products: -
Products: -
?
L-2-hydroxyisocaproate + 2,6-dichlorophenolindophenol
?
Gram-negative soil bacterium
-
Substrates: no decarboxylation
Products: -
Products: -
?
L-2-hydroxyisocaproate + 2,6-dichlorophenolindophenol
?
Gram-negative soil bacterium KY6
-
Substrates: no decarboxylation
Products: -
Products: -
?
L-lactate + O2
pyruvate + H2O2
Substrates: -
Products: -
Products: -
?
L-lactate + O2
pyruvate + H2O2
Substrates: -
Products: -
Products: -
?
lactate + 2,6-dichlorophenolindophenol
?
Gram-negative soil bacterium
-
Substrates: no decarboxylation
Products: -
Products: -
?
lactate + 2,6-dichlorophenolindophenol
?
Gram-negative soil bacterium KY6
-
Substrates: no decarboxylation
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme is highly specific for L-lactate. No substrates: D-lactate, glycolate and DL-2-hydroxybutanoate
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: no substrate: D-lactate. Poor substrate: glycolate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: D-lactate. Poor substrate: glycolate
Products: -
Products: -
?
additional information
?
-
Substrates: no substrate: D-lactate. Poor substrate: glycolate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-lactate + O2
pyruvate + H2O2
Substrates: -
Products: -
Products: -
?
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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