KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Km-values for transhydrogenase reaction | Methylosinus trichosporium OB3b | |
0.125 | - |
NADH | - |
Methylosinus trichosporium OB3b |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
36000 | - |
gel filtration | Methylosinus trichosporium OB3b |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
oxidized ferredoxin + NADH | Methylosinus trichosporium OB3b | the enzyme couples electron flow from formate dehydrogenase (NAD+ requiring) to ferredoxin | reduced ferredoxin + NAD+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Methylosinus trichosporium OB3b | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Methylosinus trichosporium OB3b |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.75 | - |
- |
Methylosinus trichosporium OB3b |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme also has transhydrogenase activity which transfers electrons and protons from NADH to thionicotinamide adenine dinucleotide phosphate and from NADPH to acetylpyridine adenine dinucleotide | Methylosinus trichosporium OB3b | ? | - |
? | |
oxidized ferredoxin + NADH | the enzyme couples electron flow from formate dehydrogenase (NAD+ requiring) to ferredoxin | Methylosinus trichosporium OB3b | reduced ferredoxin + NAD+ | - |
? |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADH | specific for NADH | Methylosinus trichosporium OB3b |