Any feedback?
Literature summary extracted from
- Purification and properties of the H(+)-nicotinamide nucleotide transhydrogenase from Rhodobacter capsulatus (1991), Eur. J. Biochem., 197, 247-255.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.1.1.1 | lysophosphatidylcholine | - |
Rhodobacter capsulatus |  |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 7.1.1.1 | - |
Rhodobacter capsulatus |
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 7.1.1.1 | purified enzyme is inactivated at 4°C even in presence of dithiothreitol | Rhodobacter capsulatus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.1.1.1 | 2'-AMP | - |
Rhodobacter capsulatus | |
| 7.1.1.1 | 5'-AMP | - |
Rhodobacter capsulatus | |
| 7.1.1.1 | acetylpyridine adenine dinucleotide | - |
Rhodobacter capsulatus | |
| 7.1.1.1 | NADP+ | mixed product inhibition vs. acetylpyridine adenine dinucleotide, competitive vs. NADPH | Rhodobacter capsulatus | |
| 7.1.1.1 | NADPH | - |
Rhodobacter capsulatus | |
| 7.1.1.1 | reduced acetylpyridine adenine dinucleotide | competitive inhibition vs. oxidized acetylpyridine adenine dinucleotide, mixed inhibition vs. NADPH | Rhodobacter capsulatus | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 7.1.1.1 | 0.006 | - |
NADPH | - |
Rhodobacter capsulatus | |
| 7.1.1.1 | 0.065 | - |
oxidized 3-acetylpyridine adenine dinucleotide | - |
Rhodobacter capsulatus | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 7.1.1.1 | chromatophore | - |
Rhodobacter capsulatus | - |
- |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.1.1.1 | Ca2+ | strong activation at concentrations of approx. 7-8 mM | Rhodobacter capsulatus | |
| 7.1.1.1 | K+ | strong activation at concentrations of approx. 100 mM | Rhodobacter capsulatus | |
| 7.1.1.1 | Mg2+ | strong activation at concentrations of approx. 3-7 mM | Rhodobacter capsulatus | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 7.1.1.1 | 48000 | - |
x * 53000 + x * 48000, SDS-PAGE | Rhodobacter capsulatus |
| 7.1.1.1 | 53000 | - |
x * 53000 + x * 48000, SDS-PAGE | Rhodobacter capsulatus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 7.1.1.1 | Rhodobacter capsulatus | - |
formerly Rhodopseudomonas capsulata | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 7.1.1.1 | - |
Rhodobacter capsulatus |
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 | 3.78 | - |
- |
Rhodobacter capsulatus |
Storage Stability
| EC Number | Storage Stability | Organism |
|---|---|---|
| 7.1.1.1 | -15°C, 20 mM sodium tricine buffer, pH 7.6, 1 mM dithiothreitol, 0.2% Triton X-100, 30% glycerol, 4 weeks, no loss of activity | Rhodobacter capsulatus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.1.1.1 | NADH + NADP+ | solubilized and purified enzyme does not catalyze reduction of acetyl pyridine adenine dinucleotide by NADH in absence of NADP+ | Rhodobacter capsulatus | NAD+ + NADPH | - |
? | |
| 7.1.1.1 | NADPH + oxidized 3-acetylpyridine adenine dinucleotide + H+ [side 1] | - |
Rhodobacter capsulatus | NADP+ + reduced 3-acetylpyridine adenine dinucleotide + H+[side 2] | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 7.1.1.1 | ? | x * 53000 + x * 48000, SDS-PAGE | Rhodobacter capsulatus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.1.1.1 | additional information | no flavin cofactor, differentiation from EC 1.6.1.1. | Rhodobacter capsulatus | |
| 7.1.1.1 | NAD+ | - |
Rhodobacter capsulatus | |
| 7.1.1.1 | NADH | - |
Rhodobacter capsulatus | |
| 7.1.1.1 | NADP+ | - |
Rhodobacter capsulatus | |
| 7.1.1.1 | NADPH | - |
Rhodobacter capsulatus | |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 7.1.1.1 | 0.011 | - |
NADPH | - |
Rhodobacter capsulatus | |
| 7.1.1.1 | 0.116 | - |
acetylpyridine adenine dinucleotide | - |
Rhodobacter capsulatus | |
| 7.1.1.1 | 0.51 | - |
5'-AMP | uncompetitive inhibition vs. NADPH | Rhodobacter capsulatus | |
| 7.1.1.1 | 0.59 | - |
2'-AMP | competitive inhibition vs. NADPH | Rhodobacter capsulatus | |
| 7.1.1.1 | 0.68 | - |
5'-AMP | competitive inhibition vs. acetylpyridine adenine dinucleotide | Rhodobacter capsulatus | |
| 7.1.1.1 | 0.75 | - |
2'-AMP | competitive inhibition vs. acetylpyridine adenine dinucleotide | Rhodobacter capsulatus | |
| 7.1.1.1 | 2.03 | - |
2'-AMP | uncompetitive inhibition vs. acetylpyridine adenine dinucleotide | Rhodobacter capsulatus | |
| 7.1.1.1 | 2.63 | - |
5'-AMP | competitive inhibition vs. NADPH | Rhodobacter capsulatus | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
