EC Number   |
Protein Variants |
Reference |
|---|
   1.1.3.2 | A95G |
activity with L-lactate similar to wild-type, increased activity with longer chain L-alpha-hydroxyacids such as alpha-hydroxy-n-butyric acid, alpha-hydroxy-n-valeric acid, and also with L-mandelic acid. Reduction of the enzyme bound flavin by substrates is the rate-limiting step in A95G |
745260 |
| 1.1.3.2 | A95G |
mutant is 3fold more reactive towards 2,6-dichlorophenol-indophenol than O2, whereas wildtype is 14fold more reactive towards O2 than 2,6-dichlorophenol-indophenol. Substituted 1,4-benzoquinones are up to 5fold better electron acceptors for reaction with L-lactate-reduced A95G variant than wild-type |
744880 |
| 1.1.3.2 | A96L |
engineering the enzyme in order to minimize the effects of oxygen interference on sensor strips. Mutant A96L shows a drastic reduction in oxidase activity using molecular oxygen as the electron acceptor and a small increase in dehydrogenase activity employing an artificial electron acceptor. After immobilization on a screen-printed carbon electrode and under argon or atmospheric conditions, the response current increases linearly from 0.05 to 0.5 mM L-lactate for both wild-type and mutant A96L. Under atmospheric conditions, the response of wild-type electrode is suppressed by 9-12% due to oxygen interference. The mutant maintains 56-69% of the response current at the same L-lactate level and minimizes the relative bias error to -19% from -49% of wild-type |
744533 |
| 1.1.3.2 | A96L |
the mutant enzyme is more stable than the wild type enzyme and the N212K single mutant |
-, 762835 |
| 1.1.3.2 | 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 |
-, 762835 |
| 1.1.3.2 | 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 |
746024 |
| 1.1.3.2 | 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 |
746024 |
| 1.1.3.2 | 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 |
746024 |
| 1.1.3.2 | 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 |
746024 |
| 1.1.3.2 | more |
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 |
744092 |
