EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.1.5.12 | fluorine-19 nuclear magnetic resonance spectroscopy of 5-fluorotryptophan-labeled enzyme. The membrane-bound D-lactate dehydrogenase may have the two-domain structure of many cytoplasmic dehydrogenases but with the addition of a membrane-binding domain between the catalytic and cofactor-binding domains | Escherichia coli |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.1.5.12 | F12W | increase in activtiy | Escherichia coli |
1.1.5.12 | F176W | about 25% of wild-type vmax | Escherichia coli |
1.1.5.12 | F263W | loss of activity | Escherichia coli |
1.1.5.12 | F279W | loss of activity | Escherichia coli |
1.1.5.12 | F326W | loss of activity | Escherichia coli |
1.1.5.12 | F340W | about 35% of wild-type vmax | Escherichia coli |
1.1.5.12 | F361W | activity similar to wild-type | Escherichia coli |
1.1.5.12 | F39W | about 50% of wild-type vmax | Escherichia coli |
1.1.5.12 | F412W | loss of activity | Escherichia coli |
1.1.5.12 | F435W | about 25% of wild-type vmax | Escherichia coli |
1.1.5.12 | F490W | loss of activity | Escherichia coli |
1.1.5.12 | F544W | loss of activity | Escherichia coli |
1.1.5.12 | I152W | loss of activity | Escherichia coli |
1.1.5.12 | I193W | loss of activity | Escherichia coli |
1.1.5.12 | I99W | loss of activity | Escherichia coli |
1.1.5.12 | L110W | loss of activity | Escherichia coli |
1.1.5.12 | L203W | loss of activity | Escherichia coli |
1.1.5.12 | L456W | loss of activity | Escherichia coli |
1.1.5.12 | L517W | about 50% of wild-type vmax | Escherichia coli |
1.1.5.12 | Y243W | activity similar to wild-type | Escherichia coli |
1.1.5.12 | Y309W | loss of activity | Escherichia coli |
1.1.5.12 | Y388W | about 75% of wild-type vmax | Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.5.12 | 0.6 | - |
(R)-lactate | mutant F39W, pH 7.2, 20°C | Escherichia coli | |
1.1.5.12 | 0.9 | - |
(R)-lactate | mutant F176W, pH 7.2, 20°C | Escherichia coli | |
1.1.5.12 | 0.9 | - |
(R)-lactate | mutant F340W, pH 7.2, 20°C | Escherichia coli | |
1.1.5.12 | 1.1 | - |
(R)-lactate | mutant F435W, pH 7.2, 20°C | Escherichia coli | |
1.1.5.12 | 1.5 | - |
(R)-lactate | mutant Y243W, pH 7.2, 20°C | Escherichia coli | |
1.1.5.12 | 1.5 | - |
(R)-lactate | mutant Y388W, pH 7.2, 20°C | Escherichia coli | |
1.1.5.12 | 1.6 | - |
(R)-lactate | wild-type, pH 7.2, 20°C | Escherichia coli | |
1.1.5.12 | 1.8 | - |
(R)-lactate | mutant L517W, pH 7.2, 20°C | Escherichia coli | |
1.1.5.12 | 2.1 | - |
(R)-lactate | mutant F12W, pH 7.2, 20°C | Escherichia coli | |
1.1.5.12 | 2.3 | - |
(R)-lactate | mutant F361W, pH 7.2, 20°C | Escherichia coli |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.5.12 | Escherichia coli | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.5.12 | (R)-lactate + a quinone | - |
Escherichia coli | pyruvate + a quinol | - |
? |