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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

(S)-lactate
+
O2
=
pyruvate
+
H2O2

Synonyms

AvLOX, L-lactate oxidase, LctO, LOX

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.3 With oxygen as acceptor
                1.1.3.2 L-lactate oxidase

Engineering

Engineering on EC 1.1.3.2 - L-lactate oxidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A96L/N212K
the double mutant shows a drastic decrease compared with that of the wild type (0.16% using 20 mM L-lactate) and A96L mutant (1.9% using 20 mM L-lactate). The mutant enzyme is more stable than the wild type enzyme and the N212K single mutant. After modification by phenazine ethosulfate, the Ala96Leu/Asn212Lys double mutant shows the highest oxidation peak in the presence of L-lactate, whereas the electrodes with the phenazine ethosulfate-modified wild type or Ala96Leu mutant do not
N212K
mutant enzyme shows decreased oxidase activity
R181K
mutation in conserved residue, efficiency of reduction of the oxidized flavin by L-lactate is greatly reduced
R181K/R268K
mutation in conserved residue, efficiency of reduction of the oxidized flavin by L-lactate is greatly reduced
R181M
mutation in conserved residue, efficiency of reduction of the oxidized flavin by L-lactate is greatly reduced
R268K
mutation in conserved residue, efficiency of reduction of the oxidized flavin by L-lactate is greatly reduced. Mutation also results in a slow conversion of the 8-CH3-substituent of FMN to yield 8-formyl-FMN
S218C
introduction of a site for chemical modification, about 50% of wild-type activity
Y191A
28fold decrease in release of pyruvate, , binding of L-lactate is strongly affected
Y191F
4.7fold decrease in release of pyruvate
Y191L
19fold decrease in release of pyruvate, binding of L-lactate is strongly affected
Y215F
mutation in binding pocket, mutant shows slowed flavin reduction and oxidation by up to 33-fold. Pyruvate release is also decelerated and is the slowest step overall
Y215H Y215F
mutation in binding pocket, mutant shows slowed flavin reduction and oxidation by up to 33-fold. Pyruvate release is also decelerated
A96L
-
the mutant enzyme is more stable than the wild type enzyme and the N212K single mutant
-
A96L/N212K
-
the double mutant shows a drastic decrease compared with that of the wild type (0.16% using 20 mM L-lactate) and A96L mutant (1.9% using 20 mM L-lactate). The mutant enzyme is more stable than the wild type enzyme and the N212K single mutant. After modification by phenazine ethosulfate, the Ala96Leu/Asn212Lys double mutant shows the highest oxidation peak in the presence of L-lactate, whereas the electrodes with the phenazine ethosulfate-modified wild type or Ala96Leu mutant do not
-
N212K
-
mutant enzyme shows decreased oxidase activity
-
F212V
change in the active site to that of Arabidopsis thaliana glycolate oxidase 2, 25fold decrease in the L-lactate oxidase/glycolate oxidase activity ratio
L112W
change in the active site to that of Arabidopsis thaliana glycolate oxidase 2, 2fold decrease in the L-lactate oxidase/glycolate oxidase activity ratio
M82T
change in the active site to that of Arabidopsis thaliana glycolate oxidase 2, 10fold decrease in the L-lactate oxidase/glycolate oxidase activity ratio
M82T/L112W/F212V
change in the active site to that of Arabidopsis thaliana glycolate oxidase 2, reverse the L-lactate oxidase/glycolate oxidase activity ratio
additional information
gene variant type 2 reveals a 51-nucleotide insertion in LctO, resulting in a 17-amino-acid repeat in the gene product, and formation of an extra loop in the monomeric protein structure. Upon expression in Escherichia coli, the higher-molecular-weight type 2 enzyme exhibits higher activity. Growth rates of Streptococcus iniae expressing the type 2 enzyme are not reduced at lactate concentrations of 0.3% and 0.5%, whereas a strain expressing the type 1 enzyme exhibits reduced growth rates at these lactate concentrations