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Literature summary extracted from
- Purification and properties of reconstitutively active nicotinamide nucleotide transhydrogenase of Escherichia coli (1985), Eur. J. Biochem., 149, 517-523.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 7.1.1.1 | expressed in Escherichia coli JM83 cells | Escherichia coli |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.1.1.1 | N,N'-dicyclohexylcarbodiimide | NADH protects the enzyme against inhibition by N,N'-dicyclohexylcarbodiimide, while NADP+ , and to a lesser extent NADPH increase the rate of inhibition | Escherichia coli |  |
| 7.1.1.1 | N,N'-Dicylclohexylcarbodiimide | NADH protects from inhibition, NADP+ and to a lesser extent NADPH increase the rate of inhibition | Escherichia coli | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 7.1.1.1 | 0.023 | - |
NADPH | - |
Escherichia coli | |
| 7.1.1.1 | 0.029 | - |
NADPH | membrane-bound enzyme | Escherichia coli | |
| 7.1.1.1 | 0.033 | - |
acetylpyridine adenine dinucleotide | - |
Escherichia coli | |
| 7.1.1.1 | 0.041 | - |
acetylpyridine adenine dinucleotide | membrane-bound enzyme | Escherichia coli | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 7.1.1.1 | cytoplasmic membrane | - |
Escherichia coli | - |
- |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 7.1.1.1 | 47000 | - |
1 * 50000 + 1 * 47000, SDS-PAGE | Escherichia coli |
| 7.1.1.1 | 50000 | - |
1 * 50000 + 1 * 47000, SDS-PAGE | Escherichia coli |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.1.1.1 | NADPH + NAD+ + H+[side 1] | Escherichia coli | - |
NADP+ + NADH + H+[side 2] | - |
r | |
| 7.1.1.1 | NADPH + NAD+ + H+[side 1] | Escherichia coli W-6 | - |
NADP+ + NADH + H+[side 2] | - |
r | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 7.1.1.1 | Escherichia coli | - |
- |
- |
| 7.1.1.1 | Escherichia coli W-6 | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 7.1.1.1 | - |
Escherichia coli |
| 7.1.1.1 | the recombinant enzyme is purified by pre-extraction of the membranes with sodium cholate and Triton X-100, solubilization of the enzyme with sodium deoxycholate in the presence of 1 M potassium chloride, and centrifugation through a 1.1 M sucrose solution. The wild type enzyme is purified by phenyl Sepharose column chromatography, DEAE-Bio-Gel A column chromatography, and NAD+ agarose column chromatography | Escherichia coli |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 7.1.1.1 | 0.0013 | - |
unpurified native enzyme, at pH 7.5, temperature not specified in the publication | Escherichia coli |
| 7.1.1.1 | 0.0052 | - |
unpurified recombinant enzyme, at pH 7.5, temperature not specified in the publication | Escherichia coli |
| 7.1.1.1 | 0.022 | - |
purified native enzyme, at pH 7.5, temperature not specified in the publication | Escherichia coli |
| 7.1.1.1 | 0.0299 | - |
purified recombinant enzyme, at pH 7.5, temperature not specified in the publication | Escherichia coli |
| 7.1.1.1 | 22 | - |
partially purified enzyme from strain W6 | Escherichia coli |
| 7.1.1.1 | 29.9 | - |
purified enzyme from strain JM83 | Escherichia coli |
Storage Stability
| EC Number | Storage Stability | Organism |
|---|---|---|
| 7.1.1.1 | 4°C, 50 mM Tris-HCl, pH 7.8, 1 mM, EDTA, 1 mM, dithiothreitol, 1 week, 10% loss of activity | Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.1.1.1 | NADPH + 3-acetylpyridine-NAD+ | - |
Escherichia coli | 3-acetylpyridine-NADH + NADP+ | - |
? | |
| 7.1.1.1 | NADPH + 3-acetylpyridine-NAD+ | - |
Escherichia coli W-6 | 3-acetylpyridine-NADH + NADP+ | - |
? | |
| 7.1.1.1 | NADPH + NAD+ + H+[side 1] | - |
Escherichia coli | NADP+ + NADH + H+[side 2] | - |
r | |
| 7.1.1.1 | NADPH + NAD+ + H+[side 1] | - |
Escherichia coli W-6 | NADP+ + NADH + H+[side 2] | - |
r | |
| 7.1.1.1 | NADPH + oxidized acetyl pyridine adenine dinucleotide + H+[side 1] | - |
Escherichia coli | NADP+ + reduced acetyl pyridine adenine dinucleotide + H+[side 2] | - |
r | |
| 7.1.1.1 | NADPH + oxidized acetyl pyridine adenine dinucleotide + H+[side 1] | - |
Escherichia coli W-6 | NADP+ + reduced acetyl pyridine adenine dinucleotide + H+[side 2] | - |
r | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 7.1.1.1 | heterodimer | 1 * 50000 + 1 * 47000, SDS-PAGE | Escherichia coli |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 7.1.1.1 | nicotinamide nucleotide transhydrogenase | - |
Escherichia coli |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.1.1.1 | NAD+ | - |
Escherichia coli | |
| 7.1.1.1 | NADH | - |
Escherichia coli | |
| 7.1.1.1 | NADP+ | - |
Escherichia coli | |
| 7.1.1.1 | NADPH | - |
Escherichia coli | |
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