EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.3.2 | expression in Escherichia coli | Aerococcus viridans |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.1.3.2 | mutant A95G in complex with pyruvate, to 1.65 A resolution. Mutation leads to increased steric volume available in the active site | Aerococcus viridans |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
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 | Aerococcus viridans |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.3.2 | additional information | - |
additional information | detailed analysis of reductive and oxidative half-reaction | Aerococcus viridans |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.3.2 | Aerococcus viridans | Q44467 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.3.2 | (S)-2-hydroxybutanoate + O2 | - |
Aerococcus viridans | 2-oxobutanoate + H2O2 | - |
? | |
1.1.3.2 | (S)-lactate + O2 | - |
Aerococcus viridans | pyruvate + H2O2 | - |
? | |
1.1.3.2 | (S)-mandelic acid + O2 | - |
Aerococcus viridans | phenylpyruvate + H2O2 | - |
? |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.3.2 | 140 | - |
(S)-lactate | mutant A95G, pH 6.5, 20°C | Aerococcus viridans | |
1.1.3.2 | 140 | - |
(S)-lactate | wild-type, pH 6.5, 20°C | Aerococcus viridans |