EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.6.1.2 | 2',5'-ADP | bacteriorhodopsin co-reconstituted enzyme, 36.8% inhibition of thio-NADP+ reduction by NADH in the dark, 34.4% in the light | Escherichia coli | |
1.6.1.2 | 2'-AMP | bacteriorhodopsin co-reconstituted enzyme, 36.8% inhibition of thio-NADP+ reduction by NADH in the dark, 31.2% in the light | Escherichia coli | |
1.6.1.2 | 5'-adenosine diphosphate ribose | bacteriorhodopsin co-reconstituted enzyme, 29.6% inhibition of thio-NADP+ reduction by NADH in the dark, 13.2% in the light | Escherichia coli | |
1.6.1.2 | 5'-AMP | bacteriorhodopsin co-reconstituted enzyme, 54.6% inhibition of thio-NADP+ reduction by NADH in the dark, 24.3% in the light | Escherichia coli | |
1.6.1.2 | adenosine | bacteriorhodopsin co-reconstituted enzyme, 54.2% inhibition of thio-NADP+ reduction by NADH in the dark, 16.0% in the light | Escherichia coli | |
1.6.1.2 | NAD+ | bacteriorhodopsin co-reconstituted enzyme, 61.5% inhibition of thio-NADP+ reduction by NADH in the dark, 18.4% in the light | Escherichia coli | |
1.6.1.2 | NADPH | bacteriorhodopsin co-reconstituted enzyme, 76.9% inhibition of thio-NADP+ reduction by NADH in the dark, 57.4% in the light | Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.6.1.2 | 0.003 | - |
NADH | enzyme co-reconstituted with bacteriorhodopsin, in the light | Escherichia coli | |
1.6.1.2 | 0.012 | - |
thio-NADP+ | enzyme co-reconstituted with bacteriorhodopsin, in the dark | Escherichia coli | |
1.6.1.2 | 0.013 | - |
thio-NADP+ | enzyme co-reconstituted with bacteriorhodopsin, in the light | Escherichia coli | |
1.6.1.2 | 0.019 | - |
NADH | enzyme co-reconstituted with bacteriorhodopsin, in the dark | Escherichia coli | |
1.6.1.2 | 0.063 | - |
NADH | enzyme co-reconstituted with bacteriorhodopsin, in the presence of the uncoupler carbonyl cyanide m-chloro-phenylhydrazone | Escherichia coli | |
1.6.1.2 | 0.063 | - |
thio-NADP+ | enzyme co-reconstituted with bacteriorhodopsin, in the presence of the uncoupler carbonyl cyanide m-chloro-phenylhydrazone | Escherichia coli |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.6.1.2 | Escherichia coli | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.6.1.2 | - |
Escherichia coli |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.6.1.2 | 12 | 15 | - |
Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.6.1.2 | NADPH + oxidized 3-acetylpyridine adenine dinucleotide | the uncoupler carbonylcyanide-m-chlorophylhydrazone stimulates approx. 2fold | Escherichia coli | NADP+ + reduced 3-acetylpyridine adenine dinucleotide | - |
? | |
1.6.1.2 | thio-NADP+ + NADH | - |
Escherichia coli | thio-NADPH + NAD+ | - |
r |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.6.1.2 | 5.5 | - |
reduction of oxidized acetylpyridine adenine dinucleotide by NADH i.e. forward reaction | Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.6.1.2 | NAD+ | - |
Escherichia coli | |
1.6.1.2 | NADH | - |
Escherichia coli | |
1.6.1.2 | NADP+ | - |
Escherichia coli | |
1.6.1.2 | NADPH | - |
Escherichia coli |