Any feedback?
Information on EC 1.6.1.3 - NAD(P)+ transhydrogenase
for references in articles please use BRENDA:EC1.6.1.3Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.6.1.3 NAD(P)+ transhydrogenaseIUBMB 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)].
Specify your search results
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
nad(p)+ transhydrogenase, nadph:nad transhydrogenase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
pyridine nucleotide transhydrogenase
SthA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NADPH + NAD+ = NADP+ + NADH
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
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)].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetylpyridine-NADPH + NAD+
acetylpyridine-NADP+ + NADH
-
stereospecificity with respect to NADPH is not known
-
-
?
deamino-NADPH + NAD+
deamino-NADP+ + NADH
-
stereospecificity with respect to NADPH is not known
-
-
?
NADPH + acetylpyridine-NAD+
NADP+ + acetylpyridine-NADH
-
stereospecificity with respect to NADPH is not known
-
-
?
NADPH + deamino-NAD+
NADP+ + deamino-NADH
-
stereospecificity with respect to NADPH is not known
-
-
?
NADPH + NAD+
NADP+ + NADH
-
the enzyme catalyses the NADPH-driven reduction of NAD+
-
-
?
NADPH + NAD+
NADP+ + NADH
-
stereospecificity with respect to NADPH is not known
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NADPH + NAD+
NADP+ + NADH
-
the enzyme catalyses the NADPH-driven reduction of NAD+
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
Mn2+ does not affect appreciably the activity of the enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.56
-
cell-free extract, in 50 mM Tris/CI pH 7.5, temperature not specified in the publication
575
-
after 1027fold purification, in 50 mM Tris/CI pH 7.5, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.6 - 9.4
-
pH 7.6: about 40% of maximal activity, pH 9.4: about 70% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
mice lacking functional enzyme are characterized by lower energy expenditure rates, consistent with their well-known susceptibility to diet-induced obesity
physiological function
physiological function
-
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
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A432C
-
the mutant shows altered NADP(H) binding and domain interaction properties
G430C
-
the mutant shows altered NADP(H) binding and domain interaction properties
R425C
-
the mutant shows almost exclusively changes in the NADP(H)-binding properties, without changing the affinity for transhydrogenase domain I from Rhodospirillum rubrum
T393C
-
the mutant shows altered NADP(H) binding and domain interaction properties
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
-
there is no loss in activity when the enzyme is left overnight at room temperature
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ado-2',5'-P2-Sepharose 4B column chromatography and Sephadex 200 gel filtration
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.6.1.3)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
