Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
CaCl2 | divalent cations stimulate activity, highest stimulation observed with CaCl2 is twofold. Activity increased linearly with increasing CaCl2 concentration and reaches saturation at 40 mM | Acetobacterium woodii |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
29000 | - |
1 * 51000 (D-lactate dehydrogenase glycolate oxidase subunit GlcD) + 1 * 46000 (electron transfer flavoprotein alpha subunit) + 1 * 29000 (electron transfer flavoprotein beta), SDS-PAGE | Acetobacterium woodii |
46000 | - |
1 * 51000 (D-lactate dehydrogenase glycolate oxidase subunit GlcD) + 1 * 46000 (electron transfer flavoprotein alpha subunit) + 1 * 29000 (electron transfer flavoprotein beta), SDS-PAGE | Acetobacterium woodii |
51000 | - |
1 * 51000 (D-lactate dehydrogenase glycolate oxidase subunit GlcD) + 1 * 46000 (electron transfer flavoprotein alpha subunit) + 1 * 29000 (electron transfer flavoprotein beta), SDS-PAGE | Acetobacterium woodii |
138000 | - |
gel filtration | Acetobacterium woodii |
151000 | - |
native gel electrophoresis | Acetobacterium woodii |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
lactate + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster | Acetobacterium woodii | lactate is a common substrate for major groups of strictly anaerobic bacteria. The LDH/Etf complex of Acetobacterium woodii uses flavin-based electron confurcation to drive endergonic lactate oxidation with NAD+ as oxidant at the expense of simultaneous exergonic electron flow from reduced ferredoxin to NAD+ | pyruvate + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster | - |
r | |
lactate + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster | Acetobacterium woodii DSM 1030 | lactate is a common substrate for major groups of strictly anaerobic bacteria. The LDH/Etf complex of Acetobacterium woodii uses flavin-based electron confurcation to drive endergonic lactate oxidation with NAD+ as oxidant at the expense of simultaneous exergonic electron flow from reduced ferredoxin to NAD+ | pyruvate + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Acetobacterium woodii | H6LBB0 and H6LBB1 and H6LBS1 | H6LBB0: electron transfer flavoprotein beta subunit, H6LBB1: electron transfer flavoprotein alpha subunit, H6LBS1: D-lactate dehydrogenase subunit GlcD | - |
Acetobacterium woodii DSM 1030 | H6LBB0 and H6LBB1 and H6LBS1 | H6LBB0: electron transfer flavoprotein beta subunit, H6LBB1: electron transfer flavoprotein alpha subunit, H6LBS1: D-lactate dehydrogenase subunit GlcD | - |
Purification (Comment) | Organism |
---|---|
- |
Acetobacterium woodii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
lactate + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster | lactate is a common substrate for major groups of strictly anaerobic bacteria. The LDH/Etf complex of Acetobacterium woodii uses flavin-based electron confurcation to drive endergonic lactate oxidation with NAD+ as oxidant at the expense of simultaneous exergonic electron flow from reduced ferredoxin to NAD+ | Acetobacterium woodii | pyruvate + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster | - |
r | |
lactate + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster | pyruvate reduction to lactate with NADH as electron donor is highly exergonic | Acetobacterium woodii | pyruvate + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster | - |
r | |
lactate + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster | lactate is a common substrate for major groups of strictly anaerobic bacteria. The LDH/Etf complex of Acetobacterium woodii uses flavin-based electron confurcation to drive endergonic lactate oxidation with NAD+ as oxidant at the expense of simultaneous exergonic electron flow from reduced ferredoxin to NAD+ | Acetobacterium woodii DSM 1030 | pyruvate + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster | - |
r | |
lactate + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster | pyruvate reduction to lactate with NADH as electron donor is highly exergonic | Acetobacterium woodii DSM 1030 | pyruvate + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster | - |
r | |
pyruvate + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster | no NADH oxidation with pyruvate as electron acceptor. Only when oxidized ferredoxin is added to the system, the reaction is initiated and NADH oxidation is detected by a decrease of absorbance. NADH-dependent ferredoxin reduction is strictly dependent on the presence of lactate | Acetobacterium woodii | lactate + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster | - |
r | |
pyruvate + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster | no NADH oxidation with pyruvate as electron acceptor. Only when oxidized ferredoxin is added to the system, the reaction is initiated and NADH oxidation is detected by a decrease of absorbance. NADH-dependent ferredoxin reduction is strictly dependent on the presence of lactate | Acetobacterium woodii DSM 1030 | lactate + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster | - |
r |
Subunits | Comment | Organism |
---|---|---|
heterotrimer | 1 * 51000 (D-lactate dehydrogenase glycolate oxidase subunit GlcD) + 1 * 46000 (electron transfer flavoprotein alpha subunit) + 1 * 29000 (electron transfer flavoprotein beta), SDS-PAGE | Acetobacterium woodii |
Synonyms | Comment | Organism |
---|---|---|
LDH/Etf complex | - |
Acetobacterium woodii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | 30 | - |
Acetobacterium woodii |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
10 | 50 | 10°C: 65% of maximal activity, activity is optimal between 20 and 30°C. Activity above 30°C decreases by 20% and dropps down to only residual activity at 50°C | Acetobacterium woodii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
- |
Acetobacterium woodii |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
5.5 | 9 | activity is rather insensitive to a pH ranging from 5.5 to 9.0 | Acetobacterium woodii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | the LDH/Etf complex has three predicted FADs. FAD is required for stability and activity. FAD (0.005 mM) is present during all purification steps, as the enzyme precipitates in the absence of FAD. FMN can not substitute FAD | Acetobacterium woodii | |
[4Fe-4S]-center | the LDH/Etf complex has one predicted 4Fe-4S cluster | Acetobacterium woodii |
General Information | Comment | Organism |
---|---|---|
metabolism | lactate is a common substrate for major groups of strictly anaerobic bacteria. The LDH/Etf complex of Acetobacterium woodii uses flavin-based electron confurcation to drive endergonic lactate oxidation with NAD+ as oxidant at the expense of simultaneous exergonic electron flow from reduced ferredoxin to NAD+ | Acetobacterium woodii |