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Enzyme Nomenclature
Information on EC 1.6.1.2 - NAD(P)+ transhydrogenase (Re/Si-specific)
Word Map on EC 1.6.1.2
- 1.6.1.2
- nadp+
- rubrum
-
rhodospirillum
-
hydride
-
transhydrogenation
-
nadh-binding
-
submitochondrial
-
chromatophores
-
acetylpyridine
- thio-nadp+
-
detergent-dispersed
-
dihydronicotinamide
-
cysteine-free
-
acpyad+
-
non-energy-linked
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.6.1.2
-
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RECOMMENDED NAME
GeneOntology No.
NAD(P)+ transhydrogenase (Re/Si-specific)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NADPH + NAD+ = NADP+ + NADH
enzyme is stereospecific for the 4A hydrogen of NADH and the 4B hydrogen of NADPH; mechanism
-
NADPH + NAD+ = NADP+ + NADH
enzyme is stereospecific for the 4A hydrogen of NADH and the 4B hydrogen of NADPH
-
NADPH + NAD+ = NADP+ + NADH
enzyme is stereospecific for the 4A hydrogen of NADH and the 4B hydrogen of NADPH; mechanism
-
NADPH + NAD+ = NADP+ + NADH
mitochondrial proton-motive force accelerates the rate of NADPH formation 10-12fold and shifts the equilibrium in the direction of product formation
-
NADPH + NAD+ = NADP+ + NADH
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
NADPH:NAD+ oxidoreductase (Re/Si-specific)
The enzyme from heart mitochondria is Re-specific with respect to NAD+ and Si-specific with respect to NADP+ [cf. EC 1.6.1.1 NAD(P)+ transhydrogenase (Si-specific)].
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CAS REGISTRY NUMBER
COMMENTARY
9014-18-0
not distinguished from EC 1.6.1.1
9072-60-0
not distinguished from EC 1.6.1.1
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
392595, 392597, 392600, 392601, 392603, 392604, 392606, 392607, 392608, 392611, 392614, 392615, 392616, 392617, 392620, 392621, 392622, 392623, 392625, 392626, 392628, 392629, 392630, 392631, 392632, 392633, 392634, 392635, 392636, 392637, 392640, 392642, 392643, 392644, 392646, 392650, 392652, 392653, 392654, 392655, 392656, 392661, 392668, 657928
-
-
-
392583, 392594, 392610, 392613, 392618, 392619, 392636, 392639, 392643, 392645, 392657, 392658, 392662, 392663, 392664, 392665, 392667, 392668, 392671, 392672, 657468, 657928, 658003, 658197, 658712, 659274, 672321, 672325, 674194, 684605, 689135, 698677
-
-
strain MG1655, wild type strain and enzyme deficient mutant, mutant strain displays very poor growth rates
-
-
native and enzyme deficient mutant, mutant strain accumulates higher levels of glutathione disulfide
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
-
the enzyme uses energy from the mitochondrial proton gradient to produce high concentrations of NADPH
physiological function
malfunction
-
small interfering RNA silencing of the enzyme in PC-12 cells results in decreased cellular NADPH levels, altered redox status of the cell in terms of decreased GSH/GSSG ratios and increased H2O2 levels, thus leading to an increased redox potential (a more oxidized redox state). NNT knockdown results in a decrease of oxidative phosphorylation while anaerobic glycolysis levels remain unchanged. Decreased oxidative phosphorylation was associated with 1. inhibition of mitochondrial pyruvate dehydrogenase and succinyl-CoA:3-oxoacid CoA transferase activity, 2. reduction of NADH availability, 3. decline of mitochondrial membrane potential, and 4. decrease of ATP levels
malfunction
-
C57BL/6J mice, which have a deletion in the Nnt gene, exhibit greater resistance to acute pulmonary infection with Streptococcus pneumoniae. Macrophages from these mice generate more reactive oxygen species and establish a stronger inflammatory response to this pathogen
malfunction
-
spontaneous C57BL/6J(B6J-NntMUT) mutant mice show major redox alterations in respiring mitchondria, including an absence of transhydrogenation between NAD+ and NADP+, higher rates of H2O2 release, the spontaneous oxidation of NADPH,the poor ability to metabolize organic peroxide, and a higher susceptibility to undergo Ca2+-induced mitochondrial permeability transition. Liver mitochondria from B6J-NntMUT mice do not possess NNT activity. The mitochondria of mutant B6J-NntMUT mice exhibit increased oxidized/reduced glutathione ratios as compared to wild-type B6JUnib-NntW mice, phenotypes, overview
malfunction
-
knockdown of the enzyme inhibits the contribution of glutamine to the tricarbonic acid cycle and activates glucose catabolism in SkMel5 melanoma cells. The increase in glucose oxidation partially occurs through pyruvate carboxylase and renders NNT knockdown cells more sensitive to glucose deprivation. Importantly, knocking down NNT inhibits reductive carboxylation in SkMel5 and 786-O renal carcinoma cells. Overexpression of NNT is sufficient to stimulate glutamine oxidation and reductive carboxylation, whereas it inhibits glucose catabolism in the TCA cycle, with impairment of the NAD(P)H/NAD(P)+ ratios
malfunction
-
C57BL/6J mice, which have a deletion in the Nnt gene, exhibit greater resistance to acute pulmonary infection with Streptococcus pneumoniae. Macrophages from these mice generate more reactive oxygen species and establish a stronger inflammatory response to this pathogen
-
malfunction
-
C57BL/6J mice, which have a deletion in the Nnt gene, exhibit greater resistance to acute pulmonary infection with Streptococcus pneumoniae. Macrophages from these mice generate more reactive oxygen species and establish a stronger inflammatory response to this pathogen; knockdown of the enzyme inhibits the contribution of glutamine to the tricarbonic acid cycle and activates glucose catabolism in SkMel5 melanoma cells. The increase in glucose oxidation partially occurs through pyruvate carboxylase and renders NNT knockdown cells more sensitive to glucose deprivation. Importantly, knocking down NNT inhibits reductive carboxylation in SkMel5 and 786-O renal carcinoma cells. Overexpression of NNT is sufficient to stimulate glutamine oxidation and reductive carboxylation, whereas it inhibits glucose catabolism in the TCA cycle, with impairment of the NAD(P)H/NAD(P)+ ratios; spontaneous C57BL/6J(B6J-NntMUT) mutant mice show major redox alterations in respiring mitchondria, including an absence of transhydrogenation between NAD+ and NADP+, higher rates of H2O2 release, the spontaneous oxidation of NADPH,the poor ability to metabolize organic peroxide, and a higher susceptibility to undergo Ca2+-induced mitochondrial permeability transition. Liver mitochondria from B6J-NntMUT mice do not possess NNT activity. The mitochondria of mutant B6J-NntMUT mice exhibit increased oxidized/reduced glutathione ratios as compared to wild-type B6JUnib-NntW mice, phenotypes, overview
-
physiological function
-
crucial role of the enzyme in the maintenance of the redox environment. The proton gradient across the mitochondrial inner membrane strongly stimulates the forward reaction, i.e., the generation of NADPH. Under anaerobic and energy-deficient conditions, the reverse reaction catalyzed by NNT, i.e., the generation of NADH, also has transient effects on maintaining mitochondrial membrane potential through NADPH hydrolysis and H+ pumping, but the contribution of the backward reaction to the proton gradient is probably of little significance under physiological conditions. Oxidized cellular redox state is linked to a decline in cellular bioenergetics, overview
physiological function
-
nicotinamide nucleotide transhydrogenase, NNT, is a nuclear-encoded protein that functions as a redox-driven proton pump catalyzing the reversible reduction of NADP+ by NADH and conversion of NADH to NAD+. The enzyme acts as a modulator of macrophage inflammatory responses. The enzyme NNT is an efficient generator of NADPH required by glutathione reductase to reduce glutathione, a component necessary to decrease the buildup of reactive oxygen species
physiological function
-
the enzyme functions as a high-capacity source of mitochondrial NADPH and that its functional loss due to the Nnt mutation results in mitochondrial redox abnormalities, most notably a poor ability to sustain NADP+ and glutathione in the reduced states. The enzyme is assembled across the inner mitochondrial membrane and translocates H+ to the mitochondrial matrix as NADP+ is reduced at the expense of NADH on the matrix side. The electrochemical gradient across the inner mitochondrial membrane shifts the NNT equilibrium to the right
physiological function
-
nicotinamide nucleotide transhydrogenase is a mitochondrial enzyme that transfers reducing equivalents from NADH to NADPH
physiological function
-
mitochondrial transhydrogenation serves as a source for this NADPH. It plays a key role in larvalpupal development
physiological function
-
the enzyme plays a role in reactive oxygen species detoxification in human adrenal glands
physiological function
-
nicotinamide nucleotide transhydrogenase, NNT, is a nuclear-encoded protein that functions as a redox-driven proton pump catalyzing the reversible reduction of NADP+ by NADH and conversion of NADH to NAD+. The enzyme acts as a modulator of macrophage inflammatory responses. The enzyme NNT is an efficient generator of NADPH required by glutathione reductase to reduce glutathione, a component necessary to decrease the buildup of reactive oxygen species
-
physiological function
-
nicotinamide nucleotide transhydrogenase is a mitochondrial enzyme that transfers reducing equivalents from NADH to NADPH; nicotinamide nucleotide transhydrogenase, NNT, is a nuclear-encoded protein that functions as a redox-driven proton pump catalyzing the reversible reduction of NADP+ by NADH and conversion of NADH to NAD+. The enzyme acts as a modulator of macrophage inflammatory responses. The enzyme NNT is an efficient generator of NADPH required by glutathione reductase to reduce glutathione, a component necessary to decrease the buildup of reactive oxygen species; the enzyme functions as a high-capacity source of mitochondrial NADPH and that its functional loss due to the Nnt mutation results in mitochondrial redox abnormalities, most notably a poor ability to sustain NADP+ and glutathione in the reduced states. The enzyme is assembled across the inner mitochondrial membrane and translocates H+ to the mitochondrial matrix as NADP+ is reduced at the expense of NADH on the matrix side. The electrochemical gradient across the inner mitochondrial membrane shifts the NNT equilibrium to the right
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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
NADH + oxidized 3-acetylpyridine adenine dinucleotide
NAD+ + reduced 3-acetylpyridine adenine dinucleotide
-
-
-
-
?
NADPH + 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
-
-
-
?
NADPH + oxidized 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
H+/out + NADH + NADP+
H+/in + NAD+ + NADPH
the enzyme couples the redox reaction between NAD(H) and NADP(H) to the inward transport of protons across a membrane
-
-
?
H+/out + NADH + NADP+
H+/in + NAD+ + NADPH
-
the enzyme couples the redox reaction between NAD(H) and NADP(H) to the transport of protons across a membrane
-
-
?
NADH + NADP+
NAD+ + NADPH
-
specific for 4A site of NADH, i.e. pro-R hydrogen and 4B site of NADPH, i.e. pro-S hydrogen
-
-
NADH + NADP+
NAD+ + NADPH
-
specific for 4A site of NADH, i.e. pro-R hydrogen and 4B site of NADPH, i.e. pro-S hydrogen
-
r
NADH + NADP+
NAD+ + NADPH
-
the reaction is coupled to a transmembrane proton translocation from cytosol to mitochondria
-
-
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
-
-
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, 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
-
-
r
NADH + NADP+
NAD+ + NADPH
-
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
-
-
r
NADH + NADP+
NAD+ + NADPH
-
-
-
-
r
NADH + NADP+
NAD+ + NADPH
-
specific for 4A site of NADH, i.e. pro-R hydrogen and 4B site of NADPH, i.e. pro-S hydrogen
-
-
NADH + NADP+
NAD+ + NADPH
-
specific for 4A site of NADH, i.e. pro-R hydrogen and 4B site of NADPH, i.e. pro-S hydrogen
-
-
NADH + NADP+
NAD+ + NADPH
-
reaction is catalyzed by a mixture of recombinant domains dI and dIII of either species or by a hybrid mixture of domains I and III from both species
-
-
-
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, cellular regeneration of NADPH
-
-
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
-
-
r
NADH + NADP+
NAD+ + NADPH
-
links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, major source of NADPH
-
-
r
NADH + NADP+
NAD+ + NADPH
-
links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, provides NADPH for biosynthesis and reduction of glutathione
-
-
r
NADH + NADP+
NAD+ + NADPH
-
links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, provides NADPH for the reduction of glutathione, reverse reaction results in outward proton translocation and creation of a proton motive force
-
-
r
NADH + NADP+
NAD+ + NADPH
-
reaction is catalyzed by a mixture of recombinant human domain III and recombinant R. rubrum domain I
-
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, 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
-
-
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, provides NADPH for biosynthesis and glutathione reduction
-
-
r
NADH + NADP+
NAD+ + NADPH
-
specific for 4A site of NADH, i.e. pro-R hydrogen and 4B site of NADPH, i.e. pro-S hydrogen
-
-
NADH + NADP+
NAD+ + NADPH
-
the reaction is coupled to a transmembrane proton translocation from cytosol to mitochondria
-
-
NADH + NADP+
NAD+ + NADPH
-
the reaction is coupled to a transmembrane proton translocation from cytosol to mitochondria
-
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
-
specific for 4A site of NADH, i.e. pro-R hydrogen and 4B site of NADPH, i.e. pro-S hydrogen
-
r
NADH + NADP+
NAD+ + NADPH
-
solubilized and purified enzyme does not catalyze reduction of acetyl pyridine adenine dinucleotide by NADH in absence of NADP+
-
-
-
NADH + NADP+
NAD+ + NADPH
-
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
-
-
r
NADH + NADP+
NAD+ + NADPH
-
-
-
-
r
NADH + NADP+
NAD+ + NADPH
-
synthesis of diphosphate from phosphate in chromatophores by reverse reaction
-
-
NADH + NADP+
NAD+ + NADPH
-
specific for 4A site of NADH, i.e. pro-R hydrogen and 4B site of NADPH, i.e. pro-S hydrogen
-
r
NADH + NADP+
NAD+ + NADPH
-
reaction is catalyzed by a mixture of recombinant domains dI and dIII of either species or by a hybrid mixture of domains I and III from both species
-
-
-
NADH + NADP+
NAD+ + NADPH
-
reaction is catalyzed by a mixture of recombinant human domain III and recombinant R. rubrum domain I
-
r
NADH + NADP+
NAD+ + NADPH
-
links hydride transfer between NAD(H) and NADP(H) to the outside in translocation of protons across membrane, provides NADPH for biosynthesis and reduction of glutathione, reaction is stereospecific between th 4A position of NAD(H) to the 4B position of NADP(H)
-
-
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
-
-
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
-
-
r
NADH + NADP+
NAD+ + NADPH
-
links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, provides NADPH for biosynthesis and glutathione reduction
-
-
r
NADH + NADP+
NAD+ + NADPH
-
links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, provides NADPH for biosynthesis and reduction of glutathione
-
-
r
NADH + NADP+
NADPH + NAD+
-
coupled to transmembrane transport of protons from cytosol to mitochondria
-
r
NADH + NADP+
NADPH + NAD+
-
coupled to transmembrane transport of protons from cytosol to mitochondria
-
r
NADH + NADP+
NADPH + NAD+
-
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
-
-
?
NADP+ + NADH
NADPH + NAD+
-
lacking functional nicotinamide nucleotide transhydrogenase displays increased sensitivity to oxidative stress
-
-
?
NADP+ + NADH
NADPH + NAD+
-
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
-
-
?
NADP+ + NADH
NADPH + NAD+
-
mitochondrial transhydrogenase is stereospecific for the 4A-NADH and 4B-NADPH hydrogens
-
-
?
NADP+ + NADH
NADPH + NAD+
-
mitochondrial transhydrogenase is stereospecific for the 4A-NADH and 4B-NADPH hydrogens
-
-
?
NADPH + 3-acetylpyridine-NAD+
3-acetylpyridine-NADH + NADP+
-
-
-
-
-
NADPH + NAD+
NADP+ + NADH
-
the proton gradient across the mitochondrial inner membrane strongly stimulates the forward reaction, i.e., the generation of NADPH
-
-
r
NADPH + oxidized 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
-
-
r
NADPH + oxidized 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
-
-
r
NADPH + oxidized 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
-
-
r
NADPH + oxidized 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
enzyme also catalyzes a rapid, so called cyclic reaction, i.e. the reduction of acetylpyridine adenine dinucleotide in the presence of either NADP+ or NADPH: the NADPH/NADP+ remain permanently bound to domain III and are alternately oxidized by acetylpyridine adenine dinucleotide and then reduced by NADH in domain I
-
-
NADPH + oxidized 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
enzyme also catalyzes a rapid, so called cyclic reaction, i.e. the reduction of acetylpyridine adenine dinucleotide in the presence of either NADP+ or NADPH: the NADPH/NADP+ remain permanently bound to domain III and are alternately oxidized by acetylpyridine adenine dinucleotide and then reduced by NADH in domain I
-
-
NADPH + oxidized 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
-
-
r
NADPH + oxidized 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
-
-
r
NADPH + oxidized 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
-
-
r
NADPH + oxidized 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
the uncoupler carbonylcyanide-m-chlorophylhydrazone stimulates approx. 2fold
-
-
-
NADPH + oxidized 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
enzyme also catalyzes a rapid, so called cyclic reaction, i.e. the reduction of acetylpyridine adenine dinucleotide in the presence of either NADP+ or NADPH: the NADPH/NADP+ remain permanently bound to domain III and are alternately oxidized by acetylpyridine adenine dinucleotide and then reduced by NADH in domain I
-
-
NADPH + oxidized 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
-
-
r
NADPH + oxidized 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
-
-
-
?
NADPH + oxidized 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
-
-
-
?
NADPH + oxidized 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
catalyzed by a mixture of purified recombinant domains I and III
-
r
NADPH + oxidized 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
enzyme also catalyzes a rapid, so called cyclic reaction, i.e. the reduction of acetylpyridine adenine dinucleotide in the presence of either NADP+ or NADPH: the NADPH/NADP+ remain permanently bound to domain III and are alternately oxidized by acetylpyridine adenine dinucleotide and then reduced by NADH in domain I
-
-
NADPH + oxidized 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
enzyme also catalyzes a rapid, so called cyclic reaction, i.e. the reduction of acetylpyridine adenine dinucleotide in the presence of either NADP+ or NADPH: the NADPH/NADP+ remain permanently bound to domain III and are alternately oxidized by acetylpyridine adenine dinucleotide and then reduced by NADH in domain I
-
-
additional information
?
-
-
NADP(H) binding leads to perturbation of a deeply buried part of the polypeptide backbone and to protonation of a carboxylic acid residue
-
-
-
additional information
?
-
-
with ongoing NADPH and NAD+ generation, the proton-translocating, mitochondrial transhydrogenase can serve as an additional anaerobic phosphorylation site
-
-
-
additional information
?
-
-
diabetes is potentially linked to a defective transhydrogenase gene
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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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NATURAL SUBSTRATES
NATURAL PRODUCTS
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 + oxidized 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
-
-
-
?
H+/out + NADH + NADP+
H+/in + NAD+ + NADPH
P07001
the enzyme couples the redox reaction between NAD(H) and NADP(H) to the inward transport of protons across a membrane
-
-
?
H+/out + NADH + NADP+
H+/in + NAD+ + NADPH
-
the enzyme couples the redox reaction between NAD(H) and NADP(H) to the transport of protons across a membrane
-
-
?
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
-
-
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, 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
-
-
r
NADH + NADP+
NAD+ + NADPH
-
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
-
-
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, cellular regeneration of NADPH
-
-
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
-
-
r
NADH + NADP+
NAD+ + NADPH
-
links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, major source of NADPH
-
-
r
NADH + NADP+
NAD+ + NADPH
-
links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, provides NADPH for biosynthesis and reduction of glutathione
-
-
r
NADH + NADP+
NAD+ + NADPH
-
links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, provides NADPH for the reduction of glutathione, reverse reaction results in outward proton translocation and creation of a proton motive force
-
-
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, 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
-
-
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
Q13423
links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, provides NADPH for biosynthesis and glutathione reduction
-
-
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, major source of NADPH, provides reducing agent for glutathione and is therefore 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, provides NADPH for biosynthesis and reduction of glutathione, reaction is stereospecific between th 4A position of NAD(H) to the 4B position of NADP(H)
-
-
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
Q2RSB4
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
-
-
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
-
-
r
NADH + NADP+
NAD+ + NADPH
-
links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, provides NADPH for biosynthesis and glutathione reduction
-
-
r
NADH + NADP+
NAD+ + NADPH
-
links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, provides NADPH for biosynthesis and reduction of glutathione
-
-
r
NADH + NADP+
NADPH + NAD+
-
coupled to transmembrane transport of protons from cytosol to mitochondria
-
r
NADH + NADP+
NADPH + NAD+
-
coupled to transmembrane transport of protons from cytosol to mitochondria
-
r
NADH + NADP+
NADPH + NAD+
-
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
-
-
?
NADP+ + NADH
NADPH + NAD+
-
lacking functional nicotinamide nucleotide transhydrogenase displays increased sensitivity to oxidative stress
-
-
?
NADP+ + NADH
NADPH + NAD+
-
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
-
-
?
NADPH + NAD+
NADP+ + NADH
-
the proton gradient across the mitochondrial inner membrane strongly stimulates the forward reaction, i.e., the generation of NADPH
-
-
r
additional information
?
-
-
with ongoing NADPH and NAD+ generation, the proton-translocating, mitochondrial transhydrogenase can serve as an additional anaerobic phosphorylation site
-
-
-
additional information
?
-
-
diabetes is potentially linked to a defective transhydrogenase gene
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
-
392595, 392597, 392600, 392601, 392603, 392604, 392606, 392607, 392608, 392611, 392614, 392615, 392616, 392617, 392620, 392621, 392622, 392623, 392625, 392626, 392628, 392629, 392630, 392631, 392632, 392633, 392634, 392635, 392636, 392637, 392640, 392642, 392643, 392644, 392646, 392650, 392652, 392653, 392654, 392655, 392656, 392661, 392668
NAD+
-
-
392583, 392594, 392610, 392613, 392618, 392619, 392636, 392639, 392643, 392645, 392657, 392658, 392662, 392663, 392664, 392665, 392667, 392668, 392671, 392672
NAD+
-
-
392612, 392627, 392638, 392641, 392643, 392647, 392659, 392660, 392661, 392663, 392665, 392666, 392667, 392668, 392669, 392670, 392674, 392675
NADH
-
-
392595, 392597, 392600, 392601, 392603, 392604, 392606, 392607, 392608, 392611, 392614, 392615, 392616, 392617, 392620, 392621, 392622, 392623, 392625, 392626, 392628, 392629, 392630, 392631, 392632, 392633, 392634, 392635, 392636, 392637, 392640, 392642, 392643, 392644, 392646, 392650, 392652, 392653, 392654, 392655, 392656, 392661, 392668
NADH
-
-
392583, 392594, 392610, 392613, 392618, 392619, 392636, 392639, 392643, 392645, 392657, 392658, 392662, 392663, 392664, 392665, 392667, 392668, 392671, 392672
NADH
-
-
392612, 392627, 392638, 392641, 392643, 392647, 392659, 392660, 392661, 392663, 392665, 392666, 392667, 392668, 392669, 392670, 392674, 392675
NADP+
-
-
392595, 392597, 392600, 392601, 392603, 392604, 392606, 392607, 392608, 392611, 392614, 392615, 392616, 392617, 392620, 392621, 392622, 392623, 392625, 392626, 392628, 392629, 392630, 392631, 392632, 392633, 392634, 392635, 392636, 392637, 392640, 392642, 392643, 392644, 392646, 392650, 392652, 392653, 392654, 392655, 392656, 392661, 392668
NADP+
-
-
392583, 392594, 392610, 392613, 392618, 392619, 392636, 392639, 392643, 392645, 392657, 392658, 392662, 392663, 392664, 392665, 392667, 392668, 392671, 392672
NADP+
-
-
392612, 392627, 392638, 392641, 392643, 392647, 392659, 392660, 392661, 392663, 392665, 392666, 392667, 392668, 392669, 392670, 392674, 392675
NADPH
-
-
392595, 392597, 392600, 392601, 392603, 392604, 392606, 392607, 392608, 392611, 392614, 392615, 392616, 392617, 392620, 392621, 392622, 392623, 392625, 392626, 392628, 392629, 392630, 392631, 392632, 392633, 392634, 392635, 392636, 392637, 392640, 392642, 392643, 392644, 392646, 392650, 392652, 392653, 392654, 392655, 392656, 392661, 392668
NADPH
-
-
392583, 392594, 392610, 392613, 392618, 392619, 392636, 392639, 392643, 392645, 392657, 392658, 392662, 392663, 392664, 392665, 392667, 392668, 392671, 392672
NADPH
-
-
392612, 392627, 392638, 392641, 392643, 392647, 392659, 392660, 392661, 392663, 392665, 392666, 392667, 392668, 392669, 392670, 392674, 392675
additional information
-
no flavin cofactor, differentiation from EC 1.6.1.1.
-
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
Ca2+
K+
Li+
-
not clear whether this reflects a general salt effect or a Li+ specific effect
Mg2+
Na+
Ca2+
-
required for catalytic activity; strong activation of forward reaction in the light at concentrations above 0.1 mM
K+
-
strong activation of forward reaction, i.e. the reduction of NADP+ by NADH, in the light at concentrations of approx. 50-80 mM, half-maximal activation at 10 mM
Mg2+
-
required for catalytic activity; strong activation of forward reaction, i.e. the reduction of NADP+ by NADH, in the light at concentrations above 0.1 mM
Na+
-
not clear whether this reflects a general salt effect or a Na+ specific effect
Na+
-
strong activation of forward reaction, i.e. the reduction of NADP+ by NADH, in the light at concentrations of approx. 50-80 mM, half-maximal activation at 10 mM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2',5'-ADP
-
bacteriorhodopsin co-reconstituted enzyme, 36.8% inhibition of thio-NADP+ reduction by NADH in the dark, 34.4% in the light
2,4-Dinitrophenyl-3'-dephospho-CoA
-
competitive vs. NAD+, non-competitive vs. NADPH
2-(4-maleimidoanilino)-naphthalene-6-sulfonic acid
-
0.004 mM, 2 h incubation, 75% inhibition of reverse reaction catalyzed by A348C mutant enzyme, 95% inhibition of A390C mutant enzyme after 1 h, 90% inhibition of K424C mutant enzyme after 1 h, 55% inhibition of R425C mutant enzyme after 1h
-
5'-adenosine diphosphate ribose
-
bacteriorhodopsin co-reconstituted enzyme, 29.6% inhibition of thio-NADP+ reduction by NADH in the dark, 13.2% in the light
5'-[p-(fluorosulfonyl)benzoyl]-adenosine
-
structural analog of adenosine, 2 mM, almost complete inactivation after 25 min, acetylpyridine adenine dinucleotide, NADP+, 5'-AMP, 5'-ADP or a mixture of 2'-AMP and 3'-AMP protect from inactivation, NADPH accelerates the inhibition rate, inhibition rate constant increases 50fold by increasing the pH from 6.0 to 8.5
Dansyl chloride
-
0.25 mM, almost complete inactivation after 8 min, NADP+ or NADPH accelerate inhibition rate
Dicyclohexylcarbodiimide
-
complete inhibition if 0.5 mol are bound to 1 mol of enzyme
diethyldicarbonate
-
inhibition is approx. 50% accelerated in the presence of NAD(H)
Ethoxyformic anhydride
-
2 mM, almost complete inactivation after 6 min, NADP+ or NADPH accelerate inhibition rate
fluorosulfonyl-para-benzyladenosine
-
complete inhibition if 0.5 mol are bound to 1 mol of enzyme
glutathione disulfide
-
strong, time dependent inhibition of thio-NADP+ reduction by NADH and acetylpyridine adenine dinucleotide reduction by NADPH, 50% inhibition after 40 min incubation in 26.7 mM glutathione disulfide, presence of NADPH accelerates inhibition 20fold
K+
-
200 mM, 50% inhibition at pH 7.9, 300 mM, 40% inhibition at pH 5.5, 95% at pH 8.5
N,N'-dicyclohexylcarbodiimide
-
0.3 mM significantly inhibits the the energy-linked NADH-NADP+ reactions, but not the nonenergy-linked NADH-NADP+ transhydrogenation
N-(4-Azido-2-nitrophenyl)-2-aminoethylsulfonate
-
trivial name NAP-taurine, time-dependent inactivation of reconstituted enzyme after photolysis in NAP-taurine loaded vesicles, acetylpyridine adenine dinucleotide stimulates inactivation
Na+
-
200 mM, 50% inhibition at pH 7.9, 300 mM, 40% inhibition at pH 5.5, 95% at pH 8.5
palmitoyl CoA
-
specifically interferes with Nnt activity by competition with NADPH-binding, 20% residual activity at 1 mM
Pentane-2,4-dione
-
inactivation of chromatophore complex, 156 mM, approx. 85% inactivation after 30 min, NADPH and NADP+ partially protect, half-maximal protection with 0.015 mM NADPH and 0.030 mM NADP+ respetively
pyridoxal 5'-phosphate
-
0.8 mM, almost complete inactivation after 5 min, 0.4 mM NADP+ or NADPH protect from inactivation, inhibition can be reversed to a considerable extent by L-lysine
rotenone
-
with rotenone addition, the NADH-NADP+ activity is inhibited significantly and the remaining activity reflects the nonenergy-linked reaction
S-7-nitrobenzofuran-4-yl-3'-dephospho-CoA
-
strong inhibitor, competitive vs. NAD+ and NADPH
S-7-Nitrobenzofuran-4-yl-CoA
-
strong inhibitor, competitive vs. NADPH, non-competitive vs. NAD+
additional information
-
NNT expression is 2.8fold downregulated in the vastus lateralis muscle of calorie restricted rhesus monkeys
-
2'-AMP
-
bacteriorhodopsin co-reconstituted enzyme, 36.8% inhibition of thio-NADP+ reduction by NADH in the dark, 31.2% in the light
5'-AMP
-
competitive vs acetylpyridine adenine dinucleotide, noncompetitive vs. NADPH
5'-AMP
-
bacteriorhodopsin co-reconstituted enzyme, 54.6% inhibition of thio-NADP+ reduction by NADH in the dark, 24.3% in the light
5,5'-dithiobis(2-nitrobenzoate)
-
0.02 mM, 51% inhibition, 92% inhibition in the presence of 2 mM Mg2+
5,5'-dithiobis(2-nitrobenzoate)
-
NADPH, NADP+, or NADP site-specific inhibitors protect from inactivation
adenosine
-
bacteriorhodopsin co-reconstituted enzyme, 54.2% inhibition of thio-NADP+ reduction by NADH in the dark, 16.0% in the light
Butane-2,3-dione
-
40 mM, almost complete inactivation of enzyme activity in chromatophores after 12 min, NAD+ and NADP+ partially protect, complete protection by a combination of NAD+ and NADP+
glutathione
-
inhibition of forward and reverse reaction in the presence of NADPH, no inhibition of forward reaction in the presence of NADH, 40% inhibition of reverse reaction, little or no inhibition in the absence of substrates
glutathione
-
protection by NADP+ or NAD+, presence of NADPH accelerates inhibition
methylmethane thiosulfonate
-
10 mM, approx. 80% inactivation after 320 min, approx. 40% in the presence of NADP+ or NAD+, approx. 90% in the presence of NADPH
Mg2+
-
20 mM, 50% inhibition at pH 7.0, competitive vs. NADPH and thio-NADP+, noncompetitive vs. acetylpyridine adenine dinucleotide and NADH
N,N'-Dicylclohexylcarbodiimide
-
NADH, acetylpyridine adenine dinucleotide, 5'-AMP and 5'-ADP offer nearly complete protection
N,N'-Dicylclohexylcarbodiimide
-
NADH, acetylpyridine adenine dinucleotide, 5'-AMP and 5'-ADP offer nearly complete protection; NADPH enhances the rate of inhibition by 3-4fold or more
N,N'-Dicylclohexylcarbodiimide
-
maximal inhibition at pH 6.5, NAD(H) and oxidized or reduced acetylpyridine adenine dinucleotide completely protect from inactivation, NADP+ increases the inhibition rate
N,N'-Dicylclohexylcarbodiimide
-
NADH protects from inhibition, NADP+ and to a lesser extent NADPH increase the rate of inhibition
N,N'-Dicylclohexylcarbodiimide
-
NAD+ and acetylpyridine adenine dinucleotide protect, NADP+ accelerates inhibition
N-(Ethoxycarbonyl)-2-ethoxy-1,2-dihydroquinoline
-
1.8 mM, complete inactivation after 55 min, approx. 25% inactivation after 55 min in the presence of 4 mM NMNH
N-ethylmaleimide
-
at neutral pH NADP+ and 2'-AMP partially protect while NADPH accelerates the inactivation rate, little inactivation below pH 7.5, rapid inactivation above, modification of Cys-893 is responsible for inactivation
N-ethylmaleimide
-
0.2 mM, 57% inhibition of reverse reaction in A348C mutant enzyme, 60% inhibition of K424C mutant enzyme, more than 95% inhibition of A390C mutant enzyme after 1h, R425C mutant enzyme is not inhibited
N-ethylmaleimide
-
inactivation of integral membrane bound component and soluble protein factor of enzyme from chromatophore, NADPH potentiates inactivation of the enzyme complex at low concentrations, NADP+ partially protects the intact complex and fully protects both components
NAD+
-
bacteriorhodopsin co-reconstituted enzyme, 61.5% inhibition of thio-NADP+ reduction by NADH in the dark, 18.4% in the light
NADP+
-
mixed product inhibition vs. acetylpyridine adenine dinucleotide, competitive vs. NADPH
NADPH
-
bacteriorhodopsin co-reconstituted enzyme, 76.9% inhibition of thio-NADP+ reduction by NADH in the dark, 57.4% in the light
Phenylarsine oxide
-
0.448 mM, 50% inhibition of acetylpyridine adenine dinucleotide reduction by NADPH after 1 min, 97% inhibition after 60 min, addition of glutathione restores about 50% of activity
Phenylarsine oxide
-
0.48 mM, 50% inhibition of acetylpyridine adenine dinucleotide reduction in inside-out membrane vesicles after 5 min
reduced acetylpyridine adenine dinucleotide
-
competitive vs. oxidized acetylpyridine dinucleotide, noncompetitive vs. NADPH
reduced acetylpyridine adenine dinucleotide
-
competitive inhibition vs. oxidized acetylpyridine adenine dinucleotide, mixed inhibition vs. NADPH
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
cardiolipin
-
10fold stimulation of partially purified enzyme with Escherichia coli cardiolipin
light
-
forward reaction in chromatophores is accelerated more than 20fold during illumination with photosynthetically active light
-
lysolecithin
-
aprrox. 0.3%, 150% activation of activity in chromatophore extracts
Carbonyl cyanide m-chlorophenylhydrazone
-
20fold activation of thio-NADP+ reduction by NADH in enzyme-bacteriorhodopsin vesicles in the light
Phospholipids
-
approx. 2.5fold activation 120 min after sonication with mitochondrial phospholipids
Phospholipids
-
approx. 15fold stimulation of partially purified enzyme with crude Escherichia coli lipid fraction
additional information
-
forward reaction stimulated by proton gradient from respiratory chain
-
additional information
-
forward reaction stimulated by proton gradient from respiratory chain
-
additional information
-
phosphatidylethanolamine and phosphatidylserine do not significantly stimulate transhydrogenase activity at any concentration
-
additional information
-
forward reaction stimulated by proton gradient from respiratory chain
-
additional information
-
the proton gradient across the mitochondrial inner membrane strongly stimulates the forward reaction, i.e., the generation of NADPH
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.063
NADH
-
enzyme co-reconstituted with bacteriorhodopsin, in the presence of the uncoupler carbonyl cyanide m-chloro-phenylhydrazone
0.06
oxidized acetylpyridine adenine dinucleotide
-
wild-type domain I
-
0.6
oxidized acetylpyridine adenine dinucleotide
-
Y235F mutant of domain I
-
0.8
oxidized acetylpyridine adenine dinucleotide
-
Y235N mutant of domain I
-
0.012
thio-NADP+
-
enzyme co-reconstituted with bacteriorhodopsin, in the dark
0.013
thio-NADP+
-
enzyme co-reconstituted with bacteriorhodopsin, in the light
0.063
thio-NADP+
-
enzyme co-reconstituted with bacteriorhodopsin, in the presence of the uncoupler carbonyl cyanide m-chloro-phenylhydrazone
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
oxidized acetylpyridine adenine dinucleotide
Rhodospirillum rubrum
-
kcat for recombinant domain III in the presence of saturating amounts of domain I, reduction of acetylpyridine adenine dinucleotide by NADPH
-
1.44
oxidized acetylpyridine adenine dinucleotide
Rhodospirillum rubrum
-
kcat for recombinant domain I in the presence of saturating amounts of domain III, reduction of acetylpyridine adenine dinucleotide by NADPH
-
0.0667
reduced acetylpyridine adenine dinucleotide
Escherichia coli
-
reverse reaction of wild-type domain III/R. rubrum domain I mixture
0.1
reduced acetylpyridine adenine dinucleotide
Escherichia coli
-
reverse reaction of A432C mutant domain III/R. rubrum domain I mixture
0.117
reduced acetylpyridine adenine dinucleotide
Escherichia coli
-
reverse reaction of D393C mutant domain III/R. rubrum domain I mixture
0.167
reduced acetylpyridine adenine dinucleotide
Escherichia coli
-
reverse reaction of H345C mutant domain III/R. rubrum domain I mixture; reverse reaction of R350C mutant domain III/R. rubrum domain I mixture
0.283
reduced acetylpyridine adenine dinucleotide
Escherichia coli
-
reverse reaction of K424C mutant domain III/R. rubrum domain I mixture; reverse reaction of R425C mutant domain III/R. rubrum domain I mixture
0.55
reduced acetylpyridine adenine dinucleotide
Escherichia coli
-
reverse reaction of A348C mutant domain III/R. rubrum domain I mixture
0.567
reduced acetylpyridine adenine dinucleotide
Escherichia coli
-
reverse reaction of G430C mutant domain III/R. rubrum domain I mixture
0.917
reduced acetylpyridine adenine dinucleotide
Escherichia coli
-
reverse reaction of D392C mutant domain III/R. rubrum domain I mixture
10
reduced acetylpyridine adenine dinucleotide
Escherichia coli
-
cyclic reaction of R425C mutant domain III/R. rubrum domain I mixture
11.7
reduced acetylpyridine adenine dinucleotide
Escherichia coli
-
cyclic reaction of G430C mutant domain III/R. rubrum domain I mixture
15
reduced acetylpyridine adenine dinucleotide
Escherichia coli
-
cyclic reaction of D392C mutant domain III/R. rubrum domain I mixture
20.8
reduced acetylpyridine adenine dinucleotide
Escherichia coli
-
cyclic reaction of H345C mutant domain III/R. rubrum domain I mixture
33.3
reduced acetylpyridine adenine dinucleotide
Escherichia coli
-
cyclic reaction of R350C mutant domain III/R. rubrum domain I mixture
36.7
reduced acetylpyridine adenine dinucleotide
Escherichia coli
-
cyclic reaction of K424C mutant domain III/R. rubrum domain I mixture
40
reduced acetylpyridine adenine dinucleotide
Escherichia coli
-
cyclic reaction of D393C mutant domain III/R. rubrum domain I mixture
51.7
reduced acetylpyridine adenine dinucleotide
Escherichia coli
-
cyclic reaction of A432C mutant domain III/R. rubrum domain I mixture
55
reduced acetylpyridine adenine dinucleotide
Escherichia coli
-
cyclic reaction of A348C mutant domain III/R. rubrum domain I mixture
81.7
reduced acetylpyridine adenine dinucleotide
Escherichia coli
-
cyclic reaction of wild-type domain III/R. rubrum domain I mixture
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.75
2'-AMP
-
competitive inhibition vs. acetylpyridine adenine dinucleotide
2.03
2'-AMP
-
uncompetitive inhibition vs. acetylpyridine adenine dinucleotide
0.68
5'-AMP
-
competitive inhibition vs. acetylpyridine adenine dinucleotide
0.12
reduced acetylpyridine adenine dinucleotide
-
vs. oxidized acetylpyridine adenine dinucleotide
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.1
-
membrane bound mutant enzyme with a direct linker between alpha and beta subunits; purified mutant enzyme with a direct linker between alpha and beta subunits, forward reaction
0.2
-
reduction of NADP+ by NADH driven by electron transport, cysteine-free enzyme reconstituted in membrane vesicles
0.26
-
activity in inside-out membrane vesicles at pH 7.4, presence of an uncoupler i.e. carbonylcyanide-m-chlorophylhydrazone results in 2fold stimulation
0.3
-
membrane bound mutant enzyme with a 18 residues long linker between alpha and beta subunits
0.4
-
purified mutant enzyme with a 18 residues long linker between alpha and beta subunits, forward reaction
0.42
-
reduction of NADP+ by NADH driven by electron transport, wild-type enzyme reconstituted in membrane vesicles
0.6
-
membrane bound mutant enzyme with a 32 residues long linker between alpha and beta subunits
0.7
-
purified mutant enzyme with a 32 residues long linker between alpha and beta subunits, forward reaction
0.8
-
purified mutant enzyme with a direct linker between alpha and beta subunits, reverse reaction
1.9
-
reduction of acetylpyridine adenine dinucleotide by NADPH, cysteine-free enzyme reconstituted in membrane vesicles
3
-
reduction of acetylpyridine adenine dinucleotide by NADPH, wild-type enzyme reconstituted in membrane vesicles
3.9
-
purified mutant enzyme with a 18 residues long linker between alpha and beta subunits, reverse reaction
5.5
-
purified mutant enzyme with a 32 residues long linker between alpha and beta subunits, reverse reaction
10.8
13.6
-
partially purified enzyme, assay in the presence of Escherichia coli phospholipids
14.2
42
-
purified mutant enzyme with a 32 residues long linker between alpha and beta subunits, cyclic reaction
46
-
purified mutant enzyme with a 18 residues long linker between alpha and beta subunits, cyclic reaction
50.8
-
native enzyme with acetylpyridine-NAD+ a n NADPH as substrates, pH 7.0
additional information
-
no activity detected with the insertion mutants
7
-
purified mutant enzyme with a direct linker between alpha and beta subunits, cyclic reaction
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
6
-
reverse reaction catalyzed by H91E mutant enzyme, 20% of wild-type enzyme activity
6.5
7 - 8
-
reduction of oxidized acetylpyridine adenine dinucleotide by NADPH in inside-out membrane vesicles
5.5
-
reduction of oxidized acetylpyridine adenine dinucleotide by NADH i.e. forward reaction
5.5
-
H91E mutant enzyme, optima for forward reaction below pH 5.5, 7% of wild-type enzyme activity at pH 6.0
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
titration of Escherichia coli transhydrogenase domain III with bound NADP+ or NADPH studied by NMR reveals no pH-dependent conformational change in the physiological pH range
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
bone marrow-derived, Nnt mRNA and protein are expressed in resting macrophages and down-regulated in response to inflammatory stimuli such as lipopolysaccharide. Nnt mRNA and protein expression are further repressed in fully activated macrophages; bone marrow-derived, Nnt mRNA and protein are expressed in resting macrophages and down-regulated in response to inflammatory stimuli such as lipopolysaccharide. Nnt mRNA and protein expression are repressed in fully activated macrophages
additional information
-
-
392595, 392597, 392601, 392606, 392607, 392608, 392611, 392614, 392615, 392616, 392617, 392620, 392621, 392622, 392623, 392625, 392626, 392628, 392629, 392630, 392631, 392632, 392633, 392634, 392635, 392636, 392637, 392640, 392642, 392644, 392646, 392655
-
insulin hypersecretion is associated with increased Nnt expression. It can be suggested that nicotinamide nucleotide transhydrogenase must play an important role in beta cell function
additional information
-
no or low activity in brain, prostate, seminal vesicle, spleen, testis
additional information
-
ubiquitous enzyme present in virtually all animal tissues
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enzyme is compromised of a membrane-bound component and an easily dissociable soluble factor
-
-
the enzyme is composed of three components. The dI and dIII components, which house the binding site for NAD(H) and NADP(H), respectively, are peripheral to the membrane, and dII spans the membrane
-
-
-
-
-
-
392595, 392600, 392603, 392604, 392608, 392611, 392614, 392615, 392616, 392617, 392620, 392621, 392622, 392623, 392625, 392626, 392628, 392629, 392630, 392631, 392632, 392633, 392634, 392640, 392642, 392655
-
orientation in the inner mitochondrial membrane
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
48667
-
alpha2,beta2, 2 * 53906 + 2 * 48667, calculation from nucleotide sequence
53906
-
alpha2,beta2, 2 * 53906 + 2 * 48667, calculation from nucleotide sequence
54000
-
x * 54000, immunoblot with antibodies against beef heart enzyme
109065
-
2 * 109065, monomer is composed of three domains: a 430 residue long N-terminal hydrophilic domain called dI, a 400 residue long central hydrophobic domain that intercalates into the membrane called dII, and a 200 residue long C-terminal hydrophilic domain called dIII
110000
120000
155000
206000 - 249000
-
cross-linking of purified enzyme with 10.9 mM dimethyl suberimidate dihydrochloride
210000 - 230000
210000 - 230000
-
SDS-PAGE after cross-linking with bifunctional reagents dimethyl adipimidate, dimethyl pimelimidate, dimethyl suberimidate and dithiobis(succinimidyl propionate)
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
trimer
additional information
-
the protein has three components: dI binds NADH, dIII binds NADP+, and dII spans the membrane. Transhydrogenase is a dimer of two dI-dII-dIII monomers. The two catalytic sites alternate during turnover
?
-
domain I contains the binding site for NAD+ and NADH, domain III for NADP+ and NADPH; domain I exists as a seperate polypeptide that can be removed from everted membrane vesicle i.e. chromatophores
dimer
-
2 * 109065, monomer is composed of three domains: a 430 residue long N-terminal hydrophilic domain called dI, a 400 residue long central hydrophobic domain that intercalates into the membrane called dII, and a 200 residue long C-terminal hydrophilic domain called dIII
dimer
-
2 * (40000 + 28000), SDS-PAGE, domains dIII and dI form active dimers
dimer
-
monomer is split into PntA and PntB chain, enzyme displays an overall dimeric structure
dimer
-
monomers consist of three domains dI, dII, and dIII located on two separate polypeptide chains
dimer
-
monomer is split into PntAA, PntAB, and PntB chain, enzyme displays an overall dimeric structure, dI dimers are formed in solutions of isolated dI domains
tetramer
-
alpha2,beta2, 2 * 53906 + 2 * 48667, calculation from nucleotide sequence
tetramer
-
domain I, i.e. alpha1 to alpha404, and III i.e. beta260 to beta462, are exposed to the cytosol and contain the binding sites for NAD(H) and NAD(P)H, respectively, domain II, i.e. alpha405 to alpha 510, spans the membrane
trimer
-
dI2dIII trimers formed in mixtures of recombinant dI and dIII domains
trimer
-
dimer of domain I combined with a domain III monomer, deduced from crystal structure
trimer
-
trimers of dI2dIII1 are formes in mixed solutions containing dI and dIII domains
trimer
-
mixture of isolated domains dI and dIII forms dI2dIII trimers, formation of trimers also with Q132N mutant dI domain
trimer
-
dI2dIII trimers formed in mixtures of recombinant dI and dIII domains
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospholipoprotein
-
5 mol loosely bound phospholipids, 9 mol tightly bound phospholipids
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop method, crystal structures of the NAD(H)-binding domain I of transhydrogenase in the absence as well as in the presence of oxidized and reduced substrate. The structures are determined at 1.9-2.0 A resolution
crystal structure of domain I i.e. alpha1 subunit, with and without bound NADH, 1.8 A resolution without NADH, 1.9 A with NADH bound
-
dI2dIII complex with bound NAD+ and NADP+, NADH and NADPH, and ADP-ribose and NADPH
-
dI2dIII1 complex with bound NAD+ and 1,4,5,6-tetrahydronicotinamide adenine dinucleotide phosphate the dI2dIII1 complex with bound ,4,5,6-tetrahydronicotinamide adenine dinucleotide and NADP+. dI is the NAD(H)-binding component of transhydrogenase. dIII is the NADP(H)-binding component
-
domain dIII, domain dI dimer and dI2dIII complex in the presence of limiting NADH using the vapor diffusion method
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 6
-
activity decreases as the pH approaches 6.0, although a second minor peak is evident at pH 5.0, the activity of the nonenergy-linked reaction decreases with medium acidification and activity loss is most notable at pH 4.0
695903
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
-
incubation of depleted membranes, inactivation of membrane transhydrogenase component
50
-
complete protection in the presence of NADPH, half-maximal protection with 0.01 mM NADPH
53
-
incubation for 3 min, 10 mM Mg2+ almost completely protect from inactivation
additional information
additional information
-
protection against thermal inactivation by cations, half-maximal protection is afforded at: 1-2 mM Mg2+, 2 mM Ca2+, 0.5 mM Mn2+ and 0.025 mM La3+
additional information
-
NADPH protects native enzyme from thermal inactivation, NADP+ accelerates thermal inactivation, both native and S-thionitrobenzoate derivatized enzyme are protected by Mg2+ against thermoinactivation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
cations prevent from tryptic inactivation, 95% protection with Mn2+, 89% with Ca2+ and 79% with Mg2+
-
fusion protein is substantially more stable than wild type enzyme upon storage at 4°C
-
purified enzyme is inactivated at 4°C even in presence of dithiothreitol
-
solubilized membrane component is unstable loosing all activity when stored overnight at 4°C or -70°C, stable at -70°C in the presence of 0.025 mM NADP+ for several months, inactivation by refreezing after thawing
-
trypsinolysis is stimulated several fold by NADPH and NADP+, half-maximal stimulation with 0.001-0.002 mM NADPH and 0.002-0.003 mM NADP+, Mg2+ protects from NADP+ stimulated inactivation
-
unstable, loses 30-50% activity within 48 h at 4°C, remainder of the enzyme becomes inactive after 2 weeks, complete inactivation after freezing at -20°C or -70°C overnight, enzyme is very susceptible to trypsinolysis, NADH protects from tryptic inactivation, NADPH promotes tryptic inactivation
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acetone
-
used for conversion of mitochondria to an acetone powder causes inactivation
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, 20 mM sodium tricine buffer, pH 7.6, 1 mM dithiothreitol, 0.2% Triton X-100, 30% glycerol, 4 weeks, no loss of activity
-
-70°C or 4°C, Rhodospirillum rubrum membrane component, inactivation in 1 day, stabilization by NADP+
-
4°C, 0.1 M sodium phosphate buffer, pH 7.5, 1 mM dithiothreitol, 0.05% sodium cholate
-
4°C, 50 mM Tris-HCl, pH 7.8, 1 mM, EDTA, 1 mM, dithiothreitol, 1 week, 10% loss of activity
-
4°C, fusion protein is substantially more stable than wild type enzyme upon storage
-
4°C, unsoluble component: 0.1 M glycyl-glycine buffer, pH 8.0, 10% sucrose, unstable, soluble factor: 120 h with 0.015 mM dithiothreitol stable
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatography
affinity chromatography; NaCl wash, Triton X-100 extraction, affinity chromatography on immobilized NAD+
-
purification of bacterially expressed, recombinant membrane protein fused with calmodulin-binding domains. This method allows isolation of the protein fusions in a single chromatography step using elution with the calcium chelating agent EDTA. Unlike purification of His-tagged proteins on nickel chelate, it is not sensitive to the presence of strong reducing agents (e.g., DTT). The protocol involves disruption of host bacteria by sonication, sedimentation of membranes by differential centrifugation, solubilization of membrane proteins and affinity chromatography on calmodulin-agarose. To achieve maximum purity and yield, the use of a combination of non-ionic and anionic detergents is suggested. Purification takes two working days, with an overnight wash of the column to increase the purity of the product
-
recombinant domain I
recombinant domain I and recombinant E155W and Y171W mutant domain III
-
recombinant protein
recombinant proteins
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
as Corynebacterium glutamicum does not possess membrane-integral nicotinamide nucleotide transhydrogenase, the Escherichia coli pntAB genes are expressed in the genetically defined Corynebacterium glutamicum lysine-producing strain DM1730, resulting in membrane-associated transhydrogenase activity of 0.7 U/mg proteine. Expression of the pntAB genes in Corynebacterium glutamicum improves L-lysine formation. In contrast, pntAB expression has a negative effect on growth and glutamate production of Corynebacterium glutamicum wild type
-
domain dI and His-tag fusion protein of dIII separately expressed in Escherichia coli
-
domains dIII and dI expressed in Escherichia coli, recombiant protein lacks the membrane spanning dII domain
-
expression of cysteine mutants A348C, A390C, K424C, and R425C in Escherichia coli
-
expression of domain I in Escherichia coli
expression of domain I Y235N and Y235F mutants in Escherichia coli
-
expression of wild-type domain III, T393C, R425C, G430C and A432C mutant domain III in Escherichia coli
-
fusion protein with calmodulin-binding peptide and His-tag expressed in Escherichia coli JM109
-
gene Nnt, overexpression of C-terminally V5-tagged full-length cDNA in the macrophage-like cell line RAW264.7, real-time PCR expression analysis
-
wild type dI and E155W and E155W/G173C mutants of dIII expressed in Escherichia coli
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A348C
-
mutation introduced into a cysteine-free mutant enzyme, mutant shows markedly reduced activity
A432C
-
mutation in domain III, reverse reaction in the presence of domain I from R. rubrum, 150% higher reaction rate than wild-type domain III/R. rubrum domain I mixture
C292T/C339T/C395S/C397T/C435S
-
cysteine of the alpha subunits replaced, similar activity as wild-type
C292T/C339T/C395S/C397T/C435S/C147S/C260S
-
all 7 cysteines of the enzyme, 5 localized in the alpha subunit and 2 in the beta subunit, are replaced, the cysteine-free mutant shows about 5fold more activity in the reduction of acetylpyridine adenine dinucleotide by NADH than wild-type, the cyclic reduction of acetylpyridine adenine dinucleotide by NADH via NADPH is 2-2.5fold more activ
E124C
-
domian dII, strongly reduced reverse activity, no effect on cyclic activity
G252C
G430C
-
mutation in domain III, reverse reaction in the presence of domain I from R. rubrum, 850% higher reaction rate than wild-type domain III/R. rubrum domain I mixture
H91K
H91R
-
mutation in domain II, leads to occlusion of NADP(H) at the NADP(H)-binding site of domain III
K424C
-
mutation introduced into a cysteine-free mutant enzyme, mutant shows markedly reduced activity
N222K
-
mutation in domain II, leads to occlusion of NADP(H) at the NADP(H)-binding site of domain III
N222R
-
mutation in domain II, leads to occlusion of NADP(H) at the NADP(H)-binding site of domain III
R425C
S237C
-
domian dII, slightly reduced reverse activity, no efect on cyclic activity
T393C
-
mutation in domain III, reverse reaction in the presence of domain I from R. rubrum, 175% higher reaction rate than wild-type domain III/R. rubrum domain I mixture
D135N
-
mutation has no effect in binding affinity of either NAD+ or NADH
E155W
E155W/G173C
-
dIII domain, catalytic properties are similar to the wild type dIII, increased rate of reverse reaction
Q132N
-
dI domain, no cyclic transhydrogenation activity in mixtures of domain dIII with the dI mutant, mutation has little effect on the NADH binding affinity
R127A
-
mutation strongly inhibits the rate of transhydrogenation and alters the nucleotide-binding properties of the dI protein. When dIR127A is reconstituted into the intact enzyme in membranes, transhydrogenation rates are negligible. dI is the NAD(H)-binding component of the transhydrogenase
R127M
-
mutation strongly inhibits the rate of transhydrogenation and alters the nucleotide-binding properties of the dI protein. When dIR127M is reconstituted into the intact enzyme in membranes, transhydrogenation rates are negligible. dI is the NAD(H)-binding component of the transhydrogenase
S135A
-
mutation has no effect in binding affinity of either NAD+ or NADH
Y146A
-
mutation in component dI that binds NADH. dI.Y146A more readily dissociates into monomers than wild-type dI. dI.Y146A monomers bind NADH much more weakly than dimers. dI.Y146A reconstitutes activity to dI-depleted membranes in its dimeric form but not in its monomeric form
Y146F
-
mutation in component dI that binds NADH. Wild-type dI and dI.Y146F reconstituted activity to dI-depleted membranes with similar characteristics
Y171W
-
mutation in domain III, similar catalytic activities as wild-type, used for tryptophan fluorescence measurements
Y235F
Y235N
additional information
H91K
-
mutation in domain II, leads to occlusion of NADP(H) at the NADP(H)-binding site of domain III
R425C
-
mutation introduced into a cysteine-free mutant enzyme, mutant shows markedly reduced activity
R425C
-
mutation in domain III, reverse reaction in the presence of domain I from R. rubrum, 425% higher reaction rate than wild-type domain III/R. rubrum domain I mixture
E155W
-
mutation in domain III, similar catalytic activities as wild-type, used for tryptophan fluorescence measurements
E155W
-
dIII domain, catalytic properties are similar to the wild type dIII
E155W
-
dIII domain, displays similar catalytic properties as wild type, introduced tryptophan fluorescence is sensitive to the redox state of the bound nucleotide
Y235F
-
mutation resides in the soluble NAD(H)-binding peripheral membrane subunit, i.e. domain I, reconstitution of depleted membranes with mutant domain I gives 44% of activity that is obtained with wild-type domain I reconstituted membranes
Y235F
-
mutant domain I/wild-type domain III mixtures catalyse acetylpyridine adenine dinucleotide reduction with similar rates as wild-type domain I/wild-type domain III mixtures
Y235N
-
mutation resides in the soluble NAD(H)-binding peripheral membrane subunit, i.e. domain I, reconstitution of depleted membranes with mutant domain I gives 18% of activity that is obtained with wild-type domain I reconstituted membranes
Y235N
-
mutant domain I/wild-type domain III mixtures catalyse acetylpyridine adenine dinucleotide reduction with similar rates as wild-type domain I/wild-type domain III mixtures
additional information
-
properties of a variety of mutant enzymes containing modified conserved and semiconserved basic and acidic residues in the beta subunit
additional information
-
enzyme overexpression reduces the production of inflammatory cytokines and the activation of mitogen-activated protein kinase signaling pathways in response to lipopolysaccharides. After 8 h, RAW264.7/NNT cells secrete significantly lower amounts of interleukin 6, TNF-alpha, and IL-1beta when compared to cells expressing empty vector. NNT overexpression impairs intracellular bacteria clearance. Wild-type C57BL/6J and C57BL/6J-NNT mice differed in inflammatory response within lung tissue
additional information
-
overexpression and knockdown of the enzyme in carcinoma cells, phenotypes, overview
additional information
-
enzyme overexpression reduces the production of inflammatory cytokines and the activation of mitogen-activated protein kinase signaling pathways in response to lipopolysaccharides. After 8 h, RAW264.7/NNT cells secrete significantly lower amounts of interleukin 6, TNF-alpha, and IL-1beta when compared to cells expressing empty vector. NNT overexpression impairs intracellular bacteria clearance. Wild-type C57BL/6J and C57BL/6J-NNT mice differed in inflammatory response within lung tissue
-
additional information
-
enzyme overexpression reduces the production of inflammatory cytokines and the activation of mitogen-activated protein kinase signaling pathways in response to lipopolysaccharides. After 8 h, RAW264.7/NNT cells secrete significantly lower amounts of interleukin 6, TNF-alpha, and IL-1beta when compared to cells expressing empty vector. NNT overexpression impairs intracellular bacteria clearance. Wild-type C57BL/6J and C57BL/6J-NNT mice differed in inflammatory response within lung tissue; overexpression and knockdown of the enzyme in carcinoma cells, phenotypes, overview
-
additional information
-
enzyme deficient mutants created by insertions at condon 474, 128, and 285 of ptnA
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reconstitution into liposomes
reconstitution into liposomes
-
Show AA Sequence (10014 entries)
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LINKS TO OTHER DATABASES (specific for EC-Number 1.6.1.2)
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