Literature summary for 7.1.1.1 extracted from

Lever, R.M.; Palmer, T.; Cunningham, I.J.; Cotton, N.P.J.; Jackson, J.B.
Purification and properties of the H(+)-nicotinamide nucleotide transhydrogenase from Rhodobacter capsulatus (1991), Eur. J. Biochem., 197, 247-255.

Search for more literature for 7.1.1.1

Activating Compound

Activating Compound	Comment	Organism	Structure
lysophosphatidylcholine	-	Rhodobacter capsulatus

Crystallization (Commentary)

Crystallization (Comment)	Organism
-	Rhodobacter capsulatus

General Stability

General Stability	Organism
purified enzyme is inactivated at 4°C even in presence of dithiothreitol	Rhodobacter capsulatus

Inhibitors

Inhibitors	Comment	Organism	Structure
2'-AMP	-	Rhodobacter capsulatus
5'-AMP	-	Rhodobacter capsulatus
acetylpyridine adenine dinucleotide	-	Rhodobacter capsulatus
NADP+	mixed product inhibition vs. acetylpyridine adenine dinucleotide, competitive vs. NADPH	Rhodobacter capsulatus
NADPH	-	Rhodobacter capsulatus
reduced acetylpyridine adenine dinucleotide	competitive inhibition vs. oxidized acetylpyridine adenine dinucleotide, mixed inhibition vs. NADPH	Rhodobacter capsulatus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.006	-	NADPH	-	Rhodobacter capsulatus
0.065	-	oxidized 3-acetylpyridine adenine dinucleotide	-	Rhodobacter capsulatus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
chromatophore	-	Rhodobacter capsulatus	-	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	strong activation at concentrations of approx. 7-8 mM	Rhodobacter capsulatus
K+	strong activation at concentrations of approx. 100 mM	Rhodobacter capsulatus
Mg2+	strong activation at concentrations of approx. 3-7 mM	Rhodobacter capsulatus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
48000	-	x * 53000 + x * 48000, SDS-PAGE	Rhodobacter capsulatus
53000	-	x * 53000 + x * 48000, SDS-PAGE	Rhodobacter capsulatus

Organism

Organism	UniProt	Comment	Textmining
Rhodobacter capsulatus	-	formerly Rhodopseudomonas capsulata	-

Purification (Commentary)

Purification (Comment)	Organism
-	Rhodobacter capsulatus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
3.78	-	-	Rhodobacter capsulatus

Storage Stability

Storage Stability	Organism
-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)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	-	?
NADPH + oxidized 3-acetylpyridine adenine dinucleotide + H+ [side 1]	-	Rhodobacter capsulatus	NADP+ + reduced 3-acetylpyridine adenine dinucleotide + H+[side 2]	-	?

Subunits

Subunits	Comment	Organism
?	x * 53000 + x * 48000, SDS-PAGE	Rhodobacter capsulatus

Cofactor

Cofactor	Comment	Organism	Structure
additional information	no flavin cofactor, differentiation from EC 1.6.1.1.	Rhodobacter capsulatus
NAD+	-	Rhodobacter capsulatus
NADH	-	Rhodobacter capsulatus
NADP+	-	Rhodobacter capsulatus
NADPH	-	Rhodobacter capsulatus

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.011	-	NADPH	-	Rhodobacter capsulatus
0.116	-	acetylpyridine adenine dinucleotide	-	Rhodobacter capsulatus
0.51	-	5'-AMP	uncompetitive inhibition vs. NADPH	Rhodobacter capsulatus
0.59	-	2'-AMP	competitive inhibition vs. NADPH	Rhodobacter capsulatus
0.68	-	5'-AMP	competitive inhibition vs. acetylpyridine adenine dinucleotide	Rhodobacter capsulatus
0.75	-	2'-AMP	competitive inhibition vs. acetylpyridine adenine dinucleotide	Rhodobacter capsulatus
2.03	-	2'-AMP	uncompetitive inhibition vs. acetylpyridine adenine dinucleotide	Rhodobacter capsulatus
2.63	-	5'-AMP	competitive inhibition vs. NADPH	Rhodobacter capsulatus

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Release 2023.1 (January 2023)