Application | Comment | Organism |
---|---|---|
environmental protection | the reductive pathway of the enzyme resulting in formation of less toxic Cr(III)-species is suggested to be the most important among possible mechanisms for chromate biodetoxification | Ogataea angusta |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2.09 | - |
(S)-lactate | pH 7.0, 20°C | Ogataea angusta |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-lactate + 2 ferricytochrome c | Ogataea angusta | - |
pyruvate + 2 ferrocytochrome c + 2 H+ | - |
? | |
(S)-lactate + 2 ferricytochrome c | Ogataea angusta C-105 | - |
pyruvate + 2 ferrocytochrome c + 2 H+ | - |
? | |
additional information | Ogataea angusta | chromate-reducing ability of enzyme-overproducing recombinant cells, the highest chromate-reducing activity of the cells is achieved in the presence of 2,6-dichlorophenolindophenol | ? | - |
? | |
additional information | Ogataea angusta C-105 | chromate-reducing ability of enzyme-overproducing recombinant cells, the highest chromate-reducing activity of the cells is achieved in the presence of 2,6-dichlorophenolindophenol | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Ogataea angusta | - |
- |
- |
Ogataea angusta C-105 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
native enzyme to homogeneity | Ogataea angusta |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
9 | - |
purified native enzyme, pH 7.5, 20°C | Ogataea angusta |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-lactate + 2 ferricytochrome c | - |
Ogataea angusta | pyruvate + 2 ferrocytochrome c + 2 H+ | - |
? | |
(S)-lactate + 2 ferricytochrome c | - |
Ogataea angusta C-105 | pyruvate + 2 ferrocytochrome c + 2 H+ | - |
? | |
(S)-lactate + K3[Fe(CN)6] | - |
Ogataea angusta | ? | - |
? | |
(S)-lactate + K3[Fe(CN)6] | - |
Ogataea angusta C-105 | ? | - |
? | |
additional information | chromate-reducing ability of enzyme-overproducing recombinant cells, the highest chromate-reducing activity of the cells is achieved in the presence of 2,6-dichlorophenolindophenol | Ogataea angusta | ? | - |
? | |
additional information | the enzyme has absolute specificity for L-lactate, yet is non-selective with respect to its electron acceptor | Ogataea angusta | ? | - |
? | |
additional information | chromate-reducing ability of enzyme-overproducing recombinant cells, the highest chromate-reducing activity of the cells is achieved in the presence of 2,6-dichlorophenolindophenol | Ogataea angusta C-105 | ? | - |
? | |
additional information | the enzyme has absolute specificity for L-lactate, yet is non-selective with respect to its electron acceptor | Ogataea angusta C-105 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
FC b2 | - |
Ogataea angusta |
flavocytochrome b2 | - |
Ogataea angusta |
L-lactate:cytochrome c-oxidoreductase | - |
Ogataea angusta |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | 24 | assay at | Ogataea angusta |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.3 | 7.5 | assay at | Ogataea angusta |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
2,6-dichlorophenolindophenol | - |
Ogataea angusta | |
ferricytochrome c | - |
Ogataea angusta |