EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.2.3 | - |
Saccharomyces cerevisiae |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.1.2.3 | A198G | turnover reduced to 50% | Saccharomyces cerevisiae |
1.1.2.3 | A198G/L230A | double mutant enzyme shows significant activity towards L-mandelate | Saccharomyces cerevisiae |
1.1.2.3 | I326A | mutant | Saccharomyces cerevisiae |
1.1.2.3 | L230A | mutant | Saccharomyces cerevisiae |
1.1.2.3 | L230G | mutant | Saccharomyces cerevisiae |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.2.3 | 0.49 | - |
L-lactate | wild type enzyme | Saccharomyces cerevisiae | |
1.1.2.3 | 38 | - |
L-lactate | A198G/L230G mutant enzyme | Saccharomyces cerevisiae |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.1.2.3 | Fe2+ | bound to enzyme | Saccharomyces cerevisiae |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.2.3 | (S)-lactate + 2 ferricytochrome c | Saccharomyces cerevisiae | can feed electrons to respiratory chain at the level of cytochrome c | pyruvate + 2 ferrocytochrome c + 2 H+ | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.2.3 | Saccharomyces cerevisiae | - |
- |
- |
EC Number | Storage Stability | Organism |
---|---|---|
1.1.2.3 | -180°C, long term storage | Saccharomyces cerevisiae |
1.1.2.3 | 4°C, precipitate from 70% saturated ammonium sulfate, under nitrogen, stable for several weeks | Saccharomyces cerevisiae |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.2.3 | (S)-lactate + 2 ferricytochrome c | - |
Saccharomyces cerevisiae | pyruvate + 2 ferrocytochrome c + 2 H+ | - |
? | |
1.1.2.3 | (S)-lactate + 2 ferricytochrome c | can feed electrons to respiratory chain at the level of cytochrome c | Saccharomyces cerevisiae | pyruvate + 2 ferrocytochrome c + 2 H+ | - |
? | |
1.1.2.3 | (S)-mandelate + ferricytochrome c | traces of activity with wild type enzyme, significant activity with A198G/L230G double mutant | Saccharomyces cerevisiae | hydroxy(phenyl)acetate + ferrocytochrome c | - |
? | |
1.1.2.3 | additional information | ferricyanide used as electron acceptor | Saccharomyces cerevisiae | ? | - |
? | |
1.1.2.3 | additional information | electron acceptors other than ferricytochrome c used | Saccharomyces cerevisiae | ? | - |
? |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.2.3 | additional information | - |
additional information | systematic determination of activity of all mutants with L-mandelate and L-lactate as substrate | Saccharomyces cerevisiae | |
1.1.2.3 | 0.02 | - |
L-Mandelate | wild type enzyme with ferricyanide as electron acceptor | Saccharomyces cerevisiae | |
1.1.2.3 | 8.5 | - |
L-Mandelate | A198G/L230G mutant enzyme with ferricyanide as electron acceptor | Saccharomyces cerevisiae | |
1.1.2.3 | 41 | - |
L-lactate | A198G/L230G mutant enzyme with ferricyanide as electron acceptor | Saccharomyces cerevisiae | |
1.1.2.3 | 400 | - |
L-lactate | wild type enzyme | Saccharomyces cerevisiae |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.2.3 | additional information | ferricyanide used as electron acceptor | Saccharomyces cerevisiae | |
1.1.2.3 | additional information | electron acceptors other than ferricytochrome c used | Saccharomyces cerevisiae |