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Literature summary for 1.6.1.1 extracted from
- Pyridine-nucleotide transhydrogenase. 5. Kinetic studies on transhydrogenase from Azotobacter vinelandii (1971), Eur. J. Biochem., 24, 72-82.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | dependency on Mg2+ concentration | Azotobacter vinelandii | |
| 0.015 | - |
NADPH | cosubstrate NAD+ | Azotobacter vinelandii |  |
| 0.025 | - |
NADH | cosubstrate NADP+ | Azotobacter vinelandii | |
| 0.03 | - |
thio-NADP+ | cosubstrate NADH | Azotobacter vinelandii | |
| 0.04 | - |
thio-NAD+ | NADPH + thio-NAD+ | Azotobacter vinelandii | |
| 0.05 | - |
thio-NAD+ | cosubstrate NADH | Azotobacter vinelandii | |
| 0.06 | - |
NADH | + thio-NAD+ | Azotobacter vinelandii | |
| 0.075 | - |
thio-NAD+ | cosubstrate NADPH | Azotobacter vinelandii | |
| 0.085 | - |
NADH | + thio-NADP+ | Azotobacter vinelandii | |
| 0.11 | - |
NAD+ | cosubstrate NADPH | Azotobacter vinelandii | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Azotobacter vinelandii | - |
- |
- |
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