Information on EC 1.6.1.3 - NAD(P)+ transhydrogenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.6.1.3
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RECOMMENDED NAME
GeneOntology No.
NAD(P)+ transhydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NADPH + NAD+ = NADP+ + NADH
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
NAD/NADH phosphorylation and dephosphorylation
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NAD metabolism
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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)].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetylpyridine-NADPH + NAD+
acetylpyridine-NADP+ + NADH
show the reaction diagram
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stereospecificity with respect to NADPH is not known
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?
deamino-NADPH + NAD+
deamino-NADP+ + NADH
show the reaction diagram
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stereospecificity with respect to NADPH is not known
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?
NADPH + acetylpyridine-NAD+
NADP+ + acetylpyridine-NADH
show the reaction diagram
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stereospecificity with respect to NADPH is not known
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?
NADPH + deamino-NAD+
NADP+ + deamino-NADH
show the reaction diagram
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stereospecificity with respect to NADPH is not known
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?
NADPH + NAD+
NADP+ + NADH
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
NADPH + NAD+
NADP+ + NADH
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
carbonyl cyanide 3-chlorophenylhydrazone
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carbonyl cyanide 4-(trifluoromethoxy)phenylhydrazone
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niclosamide
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6 - 9.4
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pH 7.6: about 40% of maximal activity, pH 9.4: about 70% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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assay at room temperature
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
421000
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gel filtration
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
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no loss in activity after 15 min, 45% loss of activity after 4 hours
722576
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, partially purified, stable for at least one month
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ado-2',5'-P2-Sepharose 4B column chromatography and Sephadex 200 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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