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Literature summary for 1.6.1.2 extracted from

  • Hu, X.; Zhang, J.W.; Persson, A.; Rydstrom, J.
    Characterization of the interaction of NADH with proton pumping E. coli transhydrogenase reconstituted in the absence and in the presence of bacteriorhodopsin (1995), Biochim. Biophys. Acta, 1229, 64-72.
    View publication on PubMed
Search for more literature for 1.6.1.2

Inhibitors

Inhibitors Comment Organism Structure
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
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
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
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
adenosine bacteriorhodopsin co-reconstituted enzyme, 54.2% inhibition of thio-NADP+ reduction by NADH in the dark, 16.0% in the light Escherichia coli
NAD+ bacteriorhodopsin co-reconstituted enzyme, 61.5% inhibition of thio-NADP+ reduction by NADH in the dark, 18.4% in the light Escherichia coli
NADPH bacteriorhodopsin co-reconstituted enzyme, 76.9% inhibition of thio-NADP+ reduction by NADH in the dark, 57.4% in the light Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.003
-
 NADH enzyme co-reconstituted with bacteriorhodopsin, in the light Escherichia coli
0.012
-
 thio-NADP+ enzyme co-reconstituted with bacteriorhodopsin, in the dark Escherichia coli
0.013
-
 thio-NADP+ enzyme co-reconstituted with bacteriorhodopsin, in the light Escherichia coli
0.019
-
 NADH enzyme co-reconstituted with bacteriorhodopsin, in the dark Escherichia coli
0.063
-
 NADH enzyme co-reconstituted with bacteriorhodopsin, in the presence of the uncoupler carbonyl cyanide m-chloro-phenylhydrazone Escherichia coli
0.063
-
 thio-NADP+ enzyme co-reconstituted with bacteriorhodopsin, in the presence of the uncoupler carbonyl cyanide m-chloro-phenylhydrazone Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
12 15
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADPH + oxidized 3-acetylpyridine adenine dinucleotide the uncoupler carbonylcyanide-m-chlorophylhydrazone stimulates approx. 2fold Escherichia coli NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
 ?
thio-NADP+ + NADH
-
 Escherichia coli thio-NADPH + NAD+
-
 r

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
 reduction of oxidized acetylpyridine adenine dinucleotide by NADH i.e. forward reaction Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Escherichia coli
NADH
-
 Escherichia coli
NADP+
-
 Escherichia coli
NADPH
-
 Escherichia coli