1.6.1.2: NAD(P)+ transhydrogenase (Re/Si-specific)
This is an abbreviated version!
For detailed information about NAD(P)+ transhydrogenase (Re/Si-specific), go to the full flat file.
Word Map on EC 1.6.1.2
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1.6.1.2
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nadp+
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rhodospirillum
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rubrum
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hydride
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transhydrogenation
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nadh-binding
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submitochondrial
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chromatophores
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acetylpyridine
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dihydronicotinamide
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isobutanol
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thio-nadp+
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acpdad+
- 1.6.1.2
- nadp+
- rhodospirillum
- rubrum
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hydride
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transhydrogenation
-
nadh-binding
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submitochondrial
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chromatophores
- acetylpyridine
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dihydronicotinamide
- isobutanol
- thio-nadp+
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acpdad+
Reaction
Synonyms
dII, dIII, energy-linked transhydrogenase, energy-linked, mitochondrial transhydrogenase, H+-thase, mitochondrial transhydrogenase, NAD transhydrogenase, NAD(P) transhydrogenase, NADH transhydrogenase, NADH-NADP-transhydrogenase, NADPH transhydrogenase, NADPH-NAD oxidoreductase, NADPH-NAD transhydrogenase, NADPH:NAD+ transhydrogenase, nicotinamide adenine dinucleotide (phosphate) transhydrogenase, nicotinamide nucleotide transhydrogenase, NNT, PNT, PntAB, proton-translocating nicotinamide nucleotide transhydrogenase, proton-translocating transhydrogenase, pyridine nucleotide transferase, pyridine nucleotide transhydrogenase, reversible mitochondrial membrane-associated transhydrogenase, transhydrogenase, transhydrogenase, nicotinamide adenine dinucleotide (phosphate)
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1.6.1.2 NAD(P)+ transhydrogenase (Re/Si-specific)Advanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 1.6.1.2 - NAD(P)+ transhydrogenase (Re/Si-specific)
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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
NADH + NADP+
NAD+ + NADPH
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links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, hydride ion equivalent is transferred from the A side of NC4 of NADH to the B side of NC4 of NADP+, provides NADPH for metabolic biosynthesis and reduction of glutathione
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-
r
NADH + NADP+
NAD+ + NADPH
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links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, important for the oxidative stress defense
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-
r
NADH + NADP+
NAD+ + NADPH
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links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, major source of NADPH, provides reducing agent for glutathione and is therefore important for the oxidative stress defense
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-
r
NADH + NADP+
NAD+ + NADPH
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links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, hydride ion equivalent is transferred from the A side of NC4 of NADH to the B side of NC4 of NADP+, provides NADPH for metabolic biosynthesis and reduction of glutathione
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r
NADH + NADP+
NAD+ + NADPH
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links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, important as source of NADPH for biosynthesis and glutathione reduction
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-
r
NADH + NADP+
NAD+ + NADPH
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links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, hydride ion equivalent is transferred from the A side of NC4 of NADH to the B side of NC4 of NADP+, provides NADPH for metabolic biosynthesis and reduction of glutathione
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-
r
NADH + NADP+
NAD+ + NADPH
links hydride transfer between NAD(H) and NADP(H) to the outside-in translocation of protons across membrane
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-
r
NADH + NADP+
NAD+ + NADPH
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links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, hydride ion equivalent is transferred from the A side of NC4 of NADH to the B side of NC4 of NADP+, provides NADPH for metabolic biosynthesis and reduction of glutathione
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-
r
NADH + NADP+
NAD+ + NADPH
-
links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, important for the oxidative stress defense
-
-
r
NADH + NADP+
NAD+ + NADPH
-
links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, important for the oxidative stress defense
-
-
r
NADH + NADP+
NAD+ + NADPH
-
links hydride transfer between NAD(H) and NADP(H) to the outside-in translocation of protons across membrane
-
-
r
NADH + NADP+
NAD+ + NADPH
links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane
-
-
r
NADH + NADP+
NAD+ + NADPH
-
links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, hydride ion equivalent is transferred from the A side of NC4 of NADH to the B side of NC4 of NADP+, provides NADPH for metabolic biosynthesis and reduction of glutathione
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-
r
NADH + NADP+
NADPH + NAD+
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coupled to transmembrane transport of protons from cytosol to mitochondria
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r
NADH + NADP+
NADPH + NAD+
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coupled to transmembrane transport of protons from cytosol to mitochondria
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r
NADH + NADP+
NADPH + NAD+
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the enzyme protects against methylviologen-dependent oxidative stress. Through a high GSH/GSSG ratio, transhydrogenase-generated NADPH contributes to a detoxification of peroxides formed from superoxide and lipid peroxidation
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-
?
NADP+ + NADH
NADPH + NAD+
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lacking functional nicotinamide nucleotide transhydrogenase displays increased sensitivity to oxidative stress
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?
NADP+ + NADH
NADPH + NAD+
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the membrane-integral nicotinamide nucleotide transhydrogenase PntAB of Escherichia coli can use the electrochemical proton gradient across the cytoplasmic membrane to drive the reduction of NADP+ via the oxidation of NADH
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-
?
NADPH + NAD+
NADP+ + NADH
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the proton gradient across the mitochondrial inner membrane strongly stimulates the forward reaction, i.e., the generation of NADPH
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r
additional information
?
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with ongoing NADPH and NAD+ generation, the proton-translocating, mitochondrial transhydrogenase can serve as an additional anaerobic phosphorylation site
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?
additional information
?
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diabetes is potentially linked to a defective transhydrogenase gene
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?
additional information
?
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the glucose intolerance and impaired insulin secretion of the C57BL/6J mouse strain results from oxidative stress due to a mutated nicotinamide nucleotide transhydrogenase. Mutation of this gene in a mouse strain with normal insulin secretion results in strong glucose intolerance
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?
additional information
?
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insulin hypersecretion is associated with increased Nnt expression. It can be suggest that nicotinamide nucleotide transhydrogenase must play an important role in beta cell function
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?
