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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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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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