1.1.3.2: L-lactate oxidase
This is an abbreviated version!
For detailed information about L-lactate oxidase, go to the full flat file.
Word Map on EC 1.1.3.2
Reaction
Synonyms
AvLOX, L-lactate oxidase, LctO, LOX
ECTree
1.1.3.2 L-lactate oxidaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.1.3.2 - L-lactate oxidase
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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
-
-
?
