EC Number | Cloned (Comment) | Organism |
---|---|---|
1.3.1.7 | Escherichia coli cells containing the plasmid pTDH1 which contains the gene encoding TDH under the control of the T7 polymerase promoter | Escherichia coli |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.93 | oxalate | forms a stable complex with Mn-tartrate dehydrogenase-NADH complexes | Pseudomonas putida | |
1.3.1.7 | oxalate | time-dependent inhibition | Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.3.1.7 | 0.032 | - |
D-malate | thio-NAD+ as coenzyme | Escherichia coli | |
1.3.1.7 | 0.049 | - |
D-malate | NAD+ as coenzyme | Escherichia coli | |
1.3.1.7 | 0.092 | - |
(+)-tartrate | thio-NAD+ as coenzyme | Escherichia coli | |
1.3.1.7 | 0.111 | - |
(+)-tartrate | NAD+ as coenzyme | Escherichia coli | |
1.3.1.7 | 0.83 | - |
(+)-tartrate | - |
Escherichia coli | |
1.3.1.7 | 0.99 | - |
D-malate | - |
Escherichia coli | |
1.3.1.7 | 1.63 | - |
D-malate | 3-acetylpyridine-NAD+ as coenzyme | Escherichia coli | |
1.3.1.7 | 2.62 | - |
(+)-tartrate | 3-acetylpyridine-NAD+ as coenzyme | Escherichia coli |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.93 | Pseudomonas putida | - |
expression by Escherichia coli | - |
1.3.1.7 | Escherichia coli | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.3.1.7 | - |
Escherichia coli |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.3.1.7 | meso-tartrate + NAD+ = dihydroxyfumarate + NADH + H+ | enzyme catalyzes 3 different chemical reactions from a single active site | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.93 | L-tartrate + NAD+ | - |
Pseudomonas putida | oxaloglycolate + NADH + H+ | - |
? | |
1.3.1.7 | D-malate + 3-acetylpyridine adenine dinucleotide | - |
Escherichia coli | pyruvate + CO2 + reduced 3-acetylpyridine adenine dinucleotide | - |
r | |
1.3.1.7 | D-malate + 3-pyridinealdehyde adenine dinucleotide | - |
Escherichia coli | pyruvate + CO2 + reduced 3-pyridinealdehyde adenine dinucleotide | - |
r | |
1.3.1.7 | D-malate + NAD+ | - |
Escherichia coli | pyruvate + CO2 + NADH | - |
r | |
1.3.1.7 | D-malate + NAD+ | - |
Escherichia coli | pyruvate + CO2 + NADH + H+ | - |
r | |
1.3.1.7 | D-malate + thio-NAD+ | - |
Escherichia coli | pyruvate + CO2 + thio-NADH | - |
r | |
1.3.1.7 | L-(+)-tartrate + NAD+ | in presence of Mn2+ and K+ (+)-tartrate is subject to NAD+-dependent oxidation to form oxaloglycolate | Escherichia coli | (3R)-oxaloglycolate + NADH | - |
? | |
1.3.1.7 | malate + NAD+ | oxidative decarboxylation in presence of Mn2+ and K+ | Escherichia coli | pyruvate + CO2 + NADH + H+ | - |
? | |
1.3.1.7 | meso-tartrate + 3-acetylpyridine-NAD+ | 3-acetylpyridine-NAD+ is a very slow substrate for TDH | Escherichia coli | D-glycerate + CO2 + ? | - |
? | |
1.3.1.7 | meso-tartrate + NAD+ | in presence of Mn2+ and K+ reaction requires only catalytic amounts of NAD+ | Escherichia coli | D-glycerate + CO2 + NADH + H+ | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.3.1.7 | tartrate dehydrogenase | - |
Escherichia coli |
1.3.1.7 | TDH | - |
Escherichia coli |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.3.1.7 | 0.417 | - |
(+)-tartrate | - |
Escherichia coli | |
1.3.1.7 | 13.3 | - |
D-malate | - |
Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.93 | NAD+ | cofactor | Pseudomonas putida | |
1.3.1.7 | 3-acetylpyridine adenine dinucleotide | APAD | Escherichia coli | |
1.3.1.7 | 3-pyridinealdehyde adenine dinucleotide | PAAD | Escherichia coli | |
1.3.1.7 | NAD+ | - |
Escherichia coli | |
1.3.1.7 | thio-NAD+ | - |
Escherichia coli |