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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

Reaction

(S)-lactate
+
O2
=
acetate
 +
CO2
 +
H2O

Synonyms

L-lactate monooxygenase, L-lactate-2-monooxygenase, lactate monooxygenase, lactate oxidase, lactate oxidative decarboxylase, lactate oxygenase, lactic oxidase, lactic oxygenase, LMO

ECTree

     1 Oxidoreductases
         1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
             1.13.12 With incorporation of one atom of oxygen (internal monooxygenases or internal mixed-function oxidases)
                1.13.12.4 lactate 2-monooxygenase

Inhibitors

Inhibitors on EC 1.13.12.4 - lactate 2-monooxygenase

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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(R)-lactate
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
2,3-epoxypropionic acid
-
-
2-Hydroxy-3-butynoate
2-Methyllactate
-
competitive inhibitor
acetate
D-lactate
-
competitive
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
formate
-
competitive inhibitor
oxalate
oxamate
-
competitive inhibitor
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
phosphate
-
competitive inhibitor
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