Any feedback?
Information on EC 1.13.12.4 - lactate 2-monooxygenase
for references in articles please use BRENDA:EC1.13.12.4Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.13.12.4 lactate 2-monooxygenaseIUBMB Comments
A flavoprotein (FMN).
Specify your search results
Word Map
- 1.13.12.4
- flavin
- co2
-
massey
-
williams
- phlei
-
flavocytochrome
- sulfite
- fmn
- smegmatis
- semiquinone
- flavoproteins
- oxalate
-
reoxidation
-
aerococcus
-
two-electron
- pyriformis
- mandelate
-
tetrahymena
- viridans
-
flavoenzymes
- d-lactate
-
sullivan
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
lactate monooxygenase, l-lactate-2-monooxygenase, lactate 2-monooxygenase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-lactate monooxygenase
-
-
-
-
L-lactate-2-monooxygenase
-
-
-
-
lactate monooxygenase
lactate oxidase
-
-
-
-
lactate oxidative decarboxylase
-
-
-
-
lactate oxygenase
-
-
-
-
lactic oxidase
-
-
-
-
lactic oxygenase
-
-
-
-
lactate monooxygenase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-lactate + O2 = acetate + CO2 + H2O
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidative decarboxylation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
KEGG
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
(S)-lactate:oxygen 2-oxidoreductase (decarboxylating)
A flavoprotein (FMN).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9028-72-2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
(S)-lactate + 2,6-dichlorophenolindophenol
pyruvate + ?
-
no decarboxylation
-
-
?
(S)-lactate + O2
pyruvate + H2O2
-
G99A-mutant, no decarboxylation
-
-
?
beta-chlorolactate + electron acceptor
pyruvate + Cl- + H2O
-
under anaerobic conditions
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FMN
-
-
FMN
-
with 5-deaza FMN the enzyme undergoes reduction by (S)-lactate but not catalytic reduction by O2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-Fluoro-2,4-dinitrobenzene
-
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
-
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
diethyl dicarbonate
-
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
-
complete inactivation, incorporation of 1 mol dinitrophenyl per catalytic site
p-chloromercuribenzoate
-
100% inhibition at 1.1 mM at pH 8 and 25°C after 30 min, excess of 2-mercaptoethanol protects
Phenylglyoxal
-
2 equivalents per subunit are required for total inactivation, in presence of competitive inhibitors inactivation is markedly reduced
Tetranitromethane
-
20 min at pH 8.0 and 1.5 mM; rapid and irreversible inactivation at 30°C, nitration of a single tyrosine per subunit, competitive inhibitors such as acetate, (R)-lactate or oxalate protect from inactivation
2-Hydroxy-3-butynoate
-
irreversible inactivator due to a covalent modification of the bound FMN
oxalate
-
transition state analog of a carbanion form of the substrate
oxalate
-
inhibition is reversible in the absence and irreversible in the presence of light
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Show AA Sequence and Transmembrane Helices (359 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
octamer
hexamer
-
6 * 54000-57000, sedimentation velocity analysis and diffusion coefficient determination
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized at 4°C in hanging drops with a reservoir solution of 0.1 M sodium citrate pH 4.6, 0.4 M lithium sulfate, and 0.4 M ammonium sulfate. Structures of Mycobacterium smegmatis wild-type enzyme and a wild-type-like C203A variant at 2.1 A and 1.7 A resolution, respectively
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G99A
-
(S)-lactate binds tighter to the G99A-mutant than to wild-type
H290Q
K266M
-
the rate of reduction with (S)-lactate is decreased compared with that of the wild-type enzyme, the mutant enzyme is virtually inactive
H290Q
-
the ability of L-lactate to reduce the enzyme flavin is abolished, whereas reoxidation of reduced enzyme with oxygen proceeds at a rate like that found in the wild type enzyme. Unlike the situation with wild type enzyme, where the transition state analog oxalate is bound tightly in a two-step reaction involving proton uptake from solution, the mutant enzyme binds oxalate weakly, in a single step reaction. Replacing the histidine has a significant effect on the ability of the enzyme to stabilize the flavin N(5)-sulfite adduct. Sulfite is bound at least 1000fold weaker than it is in the wild type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dissociation of subunits does not occur in the presence of 8 M urea and 100 mM 2-mercaptoethanol
-
dissociation of subunits occurs in the presence of 5 M guanidine hydrochloride and 100 mM 2-mercaptoethanol
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, crystalline suspension at 2-10 mg per ml for at least 6 months without loss of activity in the dark
-
4°C, crystalline suspension in 1 M sodium acetate buffer, pH 5.4, in the dark
-
5°C, crystalline suspension in ammonium sulfate, several months, no loss of activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Flashner, M.S.; Massey, V.
Flavoprotein oxygenases
Mol. Mech. Oxygen Activ. (Hayaishi, O., ed.) Academic Press, New York
245-283
1974
Mycolicibacterium phlei, Mycolicibacterium smegmatis
-
brenda
Sun, W.; Williams, C.H., Jr.; Massey, V.
Site-directed mutagenesis of glycine 99 to alanine in L-lactate monooxygenase from Mycobacterium smegmatis
J. Biol. Chem.
271
17226-17233
1996
Mycolicibacterium smegmatis
brenda
Muh, U.; Massey, V.; Williams, C.H., Jr.
Lactate Monooxygenase. I. Expression of the mycobacterial gene in Escherichia coli and site-directed mutagenesis of lysine 266
J. Biol. Chem.
269
7982-7988
1994
Mycolicibacterium smegmatis
brenda
Muh, U.; Williams, C.H., Jr.; Massey, V.
Lactate monooxygenase. II. Site-directed mutagenesis of the postulated active site base histidine 290
J. Biol. Chem.
269
7989-7993
1994
Mycolicibacterium smegmatis
brenda
Giegel, D.A.; Williams, C.H.; Massey, V.
L-Lactate 2-monooxygenase from Mycobacterium smegmatis. Cloning, nucleotide sequence, and primary structure homology within an enzyme family
J. Biol. Chem.
265
6626-6632
1990
Mycolicibacterium smegmatis
brenda
Murphy, C.J.; Shepherd, M.G.; Sullivan, P.A.
Chemical modification of L-lactate 2-monooxygenase with fluorodinitrobenzene: evidence for two essential histidine residues
Biochemistry
22
1665-1669
1983
Mycolicibacterium smegmatis
brenda
Durfor, C.N.; Cromartie, T.H.
Inactivation of L-lactate monooxygenase by nitration with tetranitromethane
Arch. Biochem. Biophys.
210
710-716
1981
Mycolicibacterium phlei
brenda
Choong, Y.S.; Massey, V.
Studies on lactate oxidase substituted with synthetic flavins. Iso-FMN lactate oxidase
J. Biol. Chem.
256
8671-8678
1981
Mycolicibacterium smegmatis
brenda
Peters, R.G.; Jones, W.C.; Cromartie, T.H.
Inactivation of L-lactate monooxygenase with 2,3-butanedione and phenylglyoxal
Biochemistry
20
2564-2571
1981
Mycolicibacterium phlei
brenda
Soon, C.Y.; Sheperd, M.G.; Sullivan, P.A.
Inactivation and modification of lactate oxidase with fluorodinitrobenzene
Biochem. J.
173
255-262
1978
Mycolicibacterium smegmatis
brenda
Soon, C.Y.; Sheperd, M.G.; Sullivan, P.A.
Modification of lactate oxidase with diethyl pyrocarbonate. Evidence for an active-site histidine residue
Biochem. J.
165
385-393
1977
Mycolicibacterium smegmatis
brenda
Sullivan, P.A.; Soon, C.Y.; Schreurs, W.J.; Cutfield, J.F.; Sheperd, M.G.
The structure of L-lactate oxidase from Mycobacterium smegmatis
Biochem. J.
165
375-383
1977
Mycolicibacterium smegmatis
brenda
Ghisla, S.; Massey, V.
Studies on the mechanism of action of the flavoenzyme lactate oxidase. Proton uptake and release during the binding of transition state analogs
J. Biol. Chem.
252
6729-6735
1977
Mycolicibacterium smegmatis
brenda
Ghisla, S.; Ogata, H.; Massey, V.; Schonbrunn, A.; Abeles, R.H.; Walsh, C.T.
Kinetic studies on the inactivation of L-lactate oxidase by [the acetylenic suicide substrate] 2-hydroxy-3-butynoate
Biochemistry
15
1791-1797
1976
Mycolicibacterium smegmatis
brenda
Takemori, S.; Katagiri, M.
Lactate oxygenase of Mycobacterium phlei
Methods Enzymol.
41B
329-333
1975
Mycolicibacterium phlei
-
brenda
Ghisla, S.; Massey, V.
Mechanism of inactivation of the flavoenzyme lactate oxidase by oxalate
J. Biol. Chem.
250
577-584
1975
Mycolicibacterium smegmatis
brenda
Averill, B.A.; Schonbrunn, A.; Abeles, R.H.; Weinstock, L.T.; Cheng, C.C.; Fisher, J.; Spencer, R.; Walsh, C.
Studies on the mechanism of Mycobacterium smegmatis L-lactate oxidase. 5-Deazaflavin mononucleotide as a coenzyme analogue
J. Biol. Chem.
250
1603-1605
1975
Mycolicibacterium smegmatis
brenda
Takemori, S.; Tajima, H.; Kawahara, F.; Nakai, Y.; Katagiri, M.
A lactate oxygenase from Mycobacterium phlei. 3. Evidence for the subunit structure
Arch. Biochem. Biophys.
160
289-303
1974
Mycolicibacterium phlei
brenda
Takemori, S.; Nakai, Y.; Nakazawa, K.; Katagiri, M.
A lactate oxygenase from Mycobacterium phlei. II. Spectral characteristics in aerobic and anaerobic reactions
Arch. Biochem. Biophys.
154
137-146
1973
Mycolicibacterium phlei
brenda
Walsh, C.; Lockridge, O.; Massey, V.; Abeles, R.
Studies on the mechanism of action of the flavoenzyme lactate oxidase. Oxidation and elimination with beta-chlorolactate
J. Biol. Chem.