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EC Tree
IUBMB Comments The enzyme catalyses the NADPH-driven reduction of NAD+. This entry stands for enzymes whose stereo-specificity with respect to NADPH is not known. [cf. EC 1.6.1.1, NAD(P)+ transhydrogenase (Si-specific) and EC 1.6.1.2 NAD(P)+ transhydrogenase (Re/Si-specific)].
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
nad(p)+ transhydrogenase, nadph:nad transhydrogenase,
more
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mitochondrial NADPH->NAD transhydrogenase
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NAD(P) transhydrogenase
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NADPH:NAD transhydrogenase
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nicotinamide nucleotide transhydrogenase
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proton-translocating transhydrogenase domain III
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pyridine nucleotide transhydrogenase
pyridine nucleotide transhydrogenase
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pyridine nucleotide transhydrogenase
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pyridine nucleotide transhydrogenase
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pyridine nucleotide transhydrogenase
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-
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SthA
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-
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NADPH + NAD+ = NADP+ + NADH
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-
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-
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NADPH:NAD+ oxidoreductase
The enzyme catalyses the NADPH-driven reduction of NAD+. This entry stands for enzymes whose stereo-specificity with respect to NADPH is not known. [cf. EC 1.6.1.1, NAD(P)+ transhydrogenase (Si-specific) and EC 1.6.1.2 NAD(P)+ transhydrogenase (Re/Si-specific)].
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acetylpyridine-NADPH + NAD+
acetylpyridine-NADP+ + NADH
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stereospecificity with respect to NADPH is not known
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-
?
deamino-NADPH + NAD+
deamino-NADP+ + NADH
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stereospecificity with respect to NADPH is not known
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-
?
NADPH + acetylpyridine-NAD+
NADP+ + acetylpyridine-NADH
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stereospecificity with respect to NADPH is not known
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-
?
NADPH + deamino-NAD+
NADP+ + deamino-NADH
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stereospecificity with respect to NADPH is not known
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-
?
NADPH + NAD+
NADP+ + NADH
NADPH + NAD+
NADP+ + NADH
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-
-
-
?
NADPH + NAD+
NADP+ + NADH
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-
-
-
?
NADPH + NAD+
NADP+ + NADH
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-
-
-
r
NADPH + NAD+
NADP+ + NADH
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-
-
-
?
NADPH + NAD+
NADP+ + NADH
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-
-
-
r
NADPH + NAD+
NADP+ + NADH
Megalodesulfovibrio gigas
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-
-
-
?
NADPH + NAD+
NADP+ + NADH
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-
-
-
?
NADPH + NAD+
NADP+ + NADH
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-
-
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r
NADPH + NAD+
NADP+ + NADH
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-
-
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r
NADPH + NAD+
NADP+ + NADH
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the enzyme catalyses the NADPH-driven reduction of NAD+
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?
NADPH + NAD+
NADP+ + NADH
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stereospecificity with respect to NADPH is not known
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?
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NADPH + NAD+
NADP+ + NADH
NADPH + NAD+
NADP+ + NADH
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-
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?
NADPH + NAD+
NADP+ + NADH
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-
-
-
?
NADPH + NAD+
NADP+ + NADH
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-
-
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r
NADPH + NAD+
NADP+ + NADH
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-
-
-
?
NADPH + NAD+
NADP+ + NADH
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-
-
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r
NADPH + NAD+
NADP+ + NADH
Megalodesulfovibrio gigas
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-
-
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?
NADPH + NAD+
NADP+ + NADH
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-
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?
NADPH + NAD+
NADP+ + NADH
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r
NADPH + NAD+
NADP+ + NADH
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r
NADPH + NAD+
NADP+ + NADH
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the enzyme catalyses the NADPH-driven reduction of NAD+
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?
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NADPH
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-
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Mn2+
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1 mM, slight stimulation
additional information
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Mn2+ does not affect appreciably the activity of the enzyme
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1,3-dicyclohexyl-1,3-diazapropa-1,2-diene
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2'-adenylic acid
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43% inhibition, activity with NADPH and NAD+
3'-adenylic acid
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37% inhibition, activity with NADPH and NAD+
5'-adenylic acid
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27% inhibition, activity with NADPH and NAD+
ADP
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48% inhibition, activity with NADPH and NAD+
Alpha-NAD+
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33% inhibition, activity with NADPH and NAD+
ATP
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22% inhibition, activity with NADPH and NAD+
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carbonyl cyanide 3-chlorophenylhydrazone
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carbonyl cyanide 4-(trifluoromethoxy)phenylhydrazone
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-
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0.56
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cell-free extract, in 50 mM Tris/CI pH 7.5, temperature not specified in the publication
575
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after 1027fold purification, in 50 mM Tris/CI pH 7.5, temperature not specified in the publication
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7.6 - 9.4
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pH 7.6: about 40% of maximal activity, pH 9.4: about 70% of maximal activity
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22
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assay at room temperature
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brenda
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brenda
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brenda
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brenda
Megalodesulfovibrio gigas
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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Megalodesulfovibrio gigas
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brenda
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brenda
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brenda
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-
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brenda
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brenda
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brenda
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brenda
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brenda
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malfunction
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mice lacking functional enzyme are characterized by lower energy expenditure rates, consistent with their well-known susceptibility to diet-induced obesity
physiological function
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the activity of NAD(P) transhydrogenase is a key element in determining the redox state of NADP and thus of Ca2+ retention and efflux from mitochondria
physiological function
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the enzyme of adult Hymenolepis diminuta physiologically couples matrix-localized, NADP-specific malic enzyme with NADH-dependent anaerobic electron transport. The enzyme acts in the translocation of protons from the matrix to the intermembrane space mitochondrial compartment
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A432C
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the mutant shows altered NADP(H) binding and domain interaction properties
G430C
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the mutant shows altered NADP(H) binding and domain interaction properties
R425C
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the mutant shows almost exclusively changes in the NADP(H)-binding properties, without changing the affinity for transhydrogenase domain I from Rhodospirillum rubrum
T393C
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the mutant shows altered NADP(H) binding and domain interaction properties
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4
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no loss in activity after 15 min, 45% loss of activity after 4 hours
722576
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22
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there is no loss in activity when the enzyme is left overnight at room temperature
55
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2.5 min, at least 90% of the activity is retained
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-15°C, partially purified, stable for at least one month
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Ado-2',5'-P2-Sepharose 4B column chromatography and Sephadex 200 gel filtration
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expressed in Escherichia coli BL21(DE3) cells
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Voordouw, G.; van der Vies, S.M.; Eweg, J.K.; Veeger, C.; van Breemen, J.F.L.; van Bruggen, E.F.J.
Pyridine nucleotide transhydrogenase from Azotobacter vinelandii. Improved purification, physical properties and subunit arrangement in purified polymers
Eur. J. Biochem.
111
347-355
1980
Azotobacter vinelandii, Azotobacter vinelandii ATCC 478
brenda
Bergkvist, A.; Johansson, C.; Johansson, T.; Rydstrm, J.; Karlsson, g.
Interactions of the NADP(H)-binding domain III of proton-translocating transhydrogenase from Escherichia coli with NADP(H) and the NAD(H)-binding domain I studied by NMR and site-directed mutagenesis
Biochemistry
39
12595-12605
2000
Escherichia coli
brenda
Keister, D.L.; San Pietro, A.; Stolzenbach, F.E.
Pyridine nucleotide transhydrogenase from spinach. I. Purification and properties
J. Biol. Chem.
235
2989-2996
1960
Spinacia oleracea
brenda
Chen, L.; LeGall, J.; Fareleira, P.; Santos, H.; Xavier, A.V.
Malate metabolism by Desulfovibrio gigas and its link to sulfate and fumarate reduction: purification of the malic enzyme and detection of NAD(P)+ transhydrogenase activity
Anaerobe
1
227-235
1995
Megalodesulfovibrio gigas
brenda
Vercesi, A.E.
The participation of NADP, the transmembrane potential and the energy-linked NAD(P) transhydrogenase in the process of Ca2+ efflux from rat liver mitochondria
Arch. Biochem. Biophys.
252
171-178
1987
Rattus norvegicus
brenda
McKelvey, J.R.; Fioravanti, C.F.
Coupling of malic enzyme and NADPH:NAD transhydrogenase in the energetics of Hymenolepis diminuta (Cestoda)
Comp. Biochem. Physiol. B
77
737-742
1984
Hymenolepis diminuta
brenda
Mercer, N.A.; McKelvey, J.R.; Fioravanti, C.F.
Hymenolepis diminuta: catalysis of transmembrane proton translocation by mitochondrial NADPH->NAD transhydrogenase
Exp. Parasitol.
91
52-58
1999
Hymenolepis diminuta
brenda
Fisher-Wellman, K.H.; Lin, C.T.; Ryan, T.E.; Reese, L.R.; Gilliam, L.A.; Cathey, B.L.; Lark, D.S.; Smith, C.D.; Muoio, D.M.; Neufer, P.D.
Pyruvate dehydrogenase complex and nicotinamide nucleotide transhydrogenase constitute an energy-consuming redox circuit
Biochem. J.
467
271-280
2015
Mus musculus
brenda
Nikel, P.I.; Perez-Pantoja, D.; de Lorenzo, V.
Pyridine nucleotide transhydrogenases enable redox balance of Pseudomonas putida during biodegradation of aromatic compounds
Environ. Microbiol.
18
3565-3582
2016
Pseudomonas putida, Pseudomonas putida KT 2240
brenda
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