Information on EC 1.13.12.4 - lactate 2-monooxygenase

for references in articles please use BRENDA:EC1.13.12.4
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The expected taxonomic range for this enzyme is: Mycolicibacterium

EC NUMBER
COMMENTARY hide
1.13.12.4
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RECOMMENDED NAME
GeneOntology No.
lactate 2-monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-lactate + O2 = acetate + CO2 + H2O
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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oxidative decarboxylation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Pyruvate metabolism
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SYSTEMATIC NAME
IUBMB Comments
(S)-lactate:oxygen 2-oxidoreductase (decarboxylating)
A flavoprotein (FMN).
CAS REGISTRY NUMBER
COMMENTARY hide
9028-72-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-lactate + 2,6-dichlorophenolindophenol
pyruvate + ?
show the reaction diagram
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no decarboxylation
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?
(S)-lactate + methylene blue
pyruvate + ?
show the reaction diagram
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?
(S)-lactate + O2
acetate + CO2 + H2O
show the reaction diagram
(S)-lactate + O2
pyruvate + H2O2
show the reaction diagram
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G99A-mutant, no decarboxylation
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?
(S)-malate + O2
oxaloacetate + H2O2
show the reaction diagram
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-
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?
2-hydroxy-3-butynoate + O2
?
show the reaction diagram
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-
-
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?
2-hydroxy-3-methylvalerate + O2
?
show the reaction diagram
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-
-
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?
2-hydroxybutyrate + O2
?
show the reaction diagram
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-
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?
2-hydroxycaproate + O2
?
show the reaction diagram
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-
-
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?
2-hydroxyisovalerate + O2
?
show the reaction diagram
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?
2-hydroxyvalerate + O2
?
show the reaction diagram
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?
beta-chlorolactate + electron acceptor
pyruvate + Cl- + H2O
show the reaction diagram
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under anaerobic conditions
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?
beta-chlorolactate + O2
chloroacetate + CO2 + H2O
show the reaction diagram
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?
beta-phenyllactate + O2
?
show the reaction diagram
DL-2-hydroxy-3-butynoate + O2
?
show the reaction diagram
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-
-
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?
DL-mandelate + O2
?
show the reaction diagram
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?
L-lactate + O2
acetate + CO2 + H2O
show the reaction diagram
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?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-lactate + O2
acetate + CO2 + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
riboflavin
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24% activity of that with FMN
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(R)-lactate
1-Fluoro-2,4-dinitrobenzene
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after 2 h at 2 mM, complete inactivation by dinitrophenylation of 2 mol of histidine residues per mol of enzyme-bound FMN, competitive inhibitors such as phosphate, nitrate and alpha-hydroxymalonate decrease the rate of inactivation
2,3-Butanedione
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90% inactivation at 50 mM after 90 min in 50 mM borate buffer, gel filtration in 50 mM phosphate buffer causes a recovery of 92% activiy
2,3-epoxypropionic acid
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2-Hydroxy-3-butynoate
2-Methyllactate
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competitive inhibitor
acetate
D-lactate
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competitive
diethyl dicarbonate
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6fold molar excess with respect to enzyme-bound FMN results in 92% inactivation after 13 min, substrate and competitive inhibitors decrease the maximum extent of inactivation to a 50%, modification of histidines
fluorodintrobenzene
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complete inactivation, incorporation of 1 mol dinitrophenyl per catalytic site
formate
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competitive inhibitor
oxalate
oxamate
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competitive inhibitor
p-chloromercuribenzoate
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100% inhibition at 1.1 mM at pH 8 and 25C after 30 min, excess of 2-mercaptoethanol protects
Phenylglyoxal
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2 equivalents per subunit are required for total inactivation, in presence of competitive inhibitors inactivation is markedly reduced
phosphate
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competitive inhibitor
Tetranitromethane
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20 min at pH 8.0 and 1.5 mM; rapid and irreversible inactivation at 30C, nitration of a single tyrosine per subunit, competitive inhibitors such as acetate, (R)-lactate or oxalate protect from inactivation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.014 - 34
(S)-lactate
50
beta-phenyl-(S)-lactate
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1.41 - 2
DL-2-hydroxy-3-butynoate
25
L-2-hydroxyisovalerate
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11.3
L-alpha-hydroxy-beta-methylvalerate
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0.055 - 0.92
O2
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0148
(S)-lactate
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4
(R)-lactate
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23
2,3-Butanedione
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6.4
2,3-epoxypropionic acid
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4
2-methyl-lactate
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11
acetate
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0.01
oxalate
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10 - 16
phosphate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
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8 * 43000, amino acid analysis
43072
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? * 43072, including FMN, amino acid analysis
43655
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8 * 43655, amino acid analysis, per mol of FMN
56000
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6 * 56000, flavin and terminal amino acid analysis
58600
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6 * 58600, electron microscopic analysis
300000
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sucrose density gradient centrifugation
340000
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gel filtration
341000
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sedimentation velocity data
345000
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sedimentation-equilibrium analysis
352000
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low speed sedimentation
370000
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sedimentation equilibrium analysis
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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? * 43072, including FMN, amino acid analysis
hexamer
octamer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
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20 min stable
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dissociation of subunits does not occur in the presence of 8 M urea and 100 mM 2-mercaptoethanol
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dissociation of subunits occurs in the presence of 5 M guanidine hydrochloride and 100 mM 2-mercaptoethanol
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0C, crystalline suspension at 2-10 mg per ml for at least 6 months without loss of activity in the dark
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4C, 1 M sodium acetate buffer, pH 5.7, in the dark
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4C, 80% saturated ammonium sulfate in the dark
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4C, crystalline suspension in 1 M sodium acetate buffer, pH 5.4, in the dark
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5C, crystalline suspension in ammonium sulfate, several months, no loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expressed in Escherichia coli BL21
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mutant enzyme H290Q expressed in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G99A
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(S)-lactate binds tighter to the G99A-mutant than to wild-type
K266M
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the rate of reduction with (S)-lactate is decreased compared with that of the wild-type enzyme, the mutant enzyme is virtually inactive
R293K
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uncoupled reaction, no decarboxylation
Y152F
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nearly as active as wild-type
Y44F
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uncoupled reaction, no decarboxylation
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