1.13.12.4: lactate 2-monooxygenase
This is an abbreviated version!
For detailed information about lactate 2-monooxygenase, go to the full flat file.
Word Map on EC 1.13.12.4
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1.13.12.4
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flavin
-
co2
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massey
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williams
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phlei
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flavocytochrome
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sulfite
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fmn
-
smegmatis
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semiquinone
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flavoproteins
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oxalate
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reoxidation
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aerococcus
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two-electron
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pyriformis
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mandelate
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tetrahymena
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viridans
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flavoenzymes
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d-lactate
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sullivan
- 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
Reaction
Synonyms
L-lactate monooxygenase, L-lactate-2-monooxygenase, lactate monooxygenase, lactate oxidase, lactate oxidative decarboxylase, lactate oxygenase, lactic oxidase, lactic oxygenase, LMO
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Inhibitors
Inhibitors on EC 1.13.12.4 - lactate 2-monooxygenase
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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
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
p-chloromercuribenzoate
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100% inhibition at 1.1 mM at pH 8 and 25°C 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
Tetranitromethane
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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
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irreversible inactivator due to a covalent modification of the bound FMN
oxalate
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transition state analog of a carbanion form of the substrate
oxalate
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inhibition is reversible in the absence and irreversible in the presence of light