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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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NADH + NADP+
NAD+ + NADPH
NADH + NADP+
NADPH + NAD+
NADH + oxidized 3-acetylpyridine adenine dinucleotide
NAD+ + reduced 3-acetylpyridine adenine dinucleotide
NADH + thio-NADP+
NAD+ + thio-NADPH
NADP+ + NADH
NADPH + NAD+
NADPH + 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
NADPH + 3-acetylpyridine-NAD(P)+
NADP+ + 3-acetylpyridine-NAD(P)H
-
-
-
-
r
NADPH + 3-acetylpyridine-NAD+
3-acetylpyridine-NADH + NADP+
-
-
-
-
?
NADPH + NAD+
NADP+ + NADH
NADPH + NAD+ + H+/in
NADP+ + NADH + H+/out
-
-
-
r
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
NADPH + oxidized 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
NMNH + thio-NADP+
NMN + thio-NADPH
-
-
-
?
thio-NADH + NADP+
thio-NAD+ + NADPH
-
poor substrate
-
-
r
thio-NADP+ + NADH
thio-NADPH + NAD+
-
-
-
-
r
additional information
?
-
NADH + NADP+
NAD+ + NADPH
-
-
-
?
NADH + NADP+
NAD+ + NADPH
-
-
-
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
-
r
NADH + NADP+
NAD+ + NADPH
-
stereospecificity of NADP+ reduction
-
?
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
-
-
-
-
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
-
-
-
-
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
-
-
-
r
NADH + NADP+
NAD+ + 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, important as source of NADPH for biosynthesis and glutathione reduction
-
-
r
NADH + NADP+
NAD+ + NADPH
-
-
-
?
NADH + NADP+
NAD+ + NADPH
-
-
-
?
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
-
inactive against 3'-analogs of NADP+
-
?
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
-
-
-
-
r
NADH + NADP+
NAD+ + NADPH
-
-
-
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
-
-
-
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
-
inactive against 3'-analogs of NADP+
-
?
NADH + NADP+
NAD+ + NADPH
-
-
-
-
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
-
-
-
-
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 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
-
-
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+
NADPH + NAD+
-
-
-
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
-
-
?
NADH + NADP+
NADPH + NAD+
-
-
-
r
NADH + NADP+
NADPH + NAD+
-
-
-
r
NADH + NADP+
NADPH + NAD+
-
-
-
r
NADH + NADP+
NADPH + NAD+
-
forward reaction
-
r
NADH + NADP+
NADPH + NAD+
-
physiological role
-
r
NADH + oxidized 3-acetylpyridine adenine dinucleotide
NAD+ + reduced 3-acetylpyridine adenine dinucleotide
-
-
-
-
?
NADH + oxidized 3-acetylpyridine adenine dinucleotide
NAD+ + reduced 3-acetylpyridine adenine dinucleotide
-
-
-
-
r
NADH + thio-NADP+
NAD+ + thio-NADPH
-
-
-
r
NADH + thio-NADP+
NAD+ + thio-NADPH
-
-
-
r
NADH + thio-NADP+
NAD+ + thio-NADPH
-
-
-
r
NADH + thio-NADP+
NAD+ + thio-NADPH
-
-
-
r
NADH + thio-NADP+
NAD+ + thio-NADPH
-
-
-
r
NADH + thio-NADP+
NAD+ + thio-NADPH
-
-
-
r
NADH + thio-NADP+
NAD+ + thio-NADPH
-
-
-
r
NADH + thio-NADP+
NAD+ + thio-NADPH
-
-
-
r
NADH + thio-NADP+
NAD+ + thio-NADPH
-
-
-
r
NADH + thio-NADP+
NAD+ + thio-NADPH
-
good substrate
-
-
r
NADP+ + NADH
NADPH + NAD+
-
-
-
-
?
NADP+ + NADH
NADPH + NAD+
-
-
-
-
r
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+
-
-
-
-
r
NADP+ + NADH
NADPH + NAD+
-
-
-
-
r
NADP+ + NADH
NADPH + NAD+
-
-
-
-
r
NADPH + 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
-
-
?
NADPH + 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
-
-
-
?
NADPH + 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
-
-
-
?
NADPH + NAD+
NADP+ + NADH
-
-
-
-
?
NADPH + NAD+
NADP+ + NADH
-
-
-
-
?
NADPH + NAD+
NADP+ + NADH
-
-
-
?
NADPH + NAD+
NADP+ + NADH
-
-
-
-
?
NADPH + NAD+
NADP+ + NADH
-
-
-
?
NADPH + NAD+
NADP+ + NADH
-
-
-
-
r
NADPH + NAD+
NADP+ + NADH
-
-
-
-
?
NADPH + NAD+
NADP+ + NADH
-
-
-
-
r
NADPH + NAD+
NADP+ + NADH
-
-
-
-
r
NADPH + NAD+
NADP+ + NADH
-
-
-
-
?
NADPH + NAD+
NADP+ + NADH
-
-
-
-
?
NADPH + NAD+
NADP+ + NADH
-
-
-
-
r
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 + NAD+
NADP+ + NADH
-
-
-
-
?
NADPH + NAD+
NADP+ + NADH
-
-
-
-
?
NADPH + NAD+
NADP+ + NADH
-
-
-
-
?
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
-
-
-
?
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
r
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
?
-
-
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.
NADH + NADP+
NAD+ + NADPH
NADH + NADP+
NADPH + NAD+
NADP+ + NADH
NADPH + NAD+
NADPH + NAD+
NADP+ + NADH
NADPH + NAD+ + H+/in
NADP+ + NADH + H+/out
-
-
-
r
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
additional information
?
-
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, 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 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 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 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, 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
-
-
r
NADH + NADP+
NADPH + NAD+
-
-
-
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
-
-
?
NADH + NADP+
NADPH + NAD+
-
-
-
r
NADH + NADP+
NADPH + NAD+
-
-
-
r
NADH + NADP+
NADPH + NAD+
-
-
-
r
NADH + NADP+
NADPH + NAD+
-
forward reaction
-
r
NADH + NADP+
NADPH + NAD+
-
physiological role
-
r
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
-
-
-
-
?
NADPH + NAD+
NADP+ + NADH
-
-
-
-
?
NADPH + NAD+
NADP+ + NADH
-
-
-
?
NADPH + NAD+
NADP+ + NADH
-
-
-
-
?
NADPH + NAD+
NADP+ + NADH
-
-
-
?
NADPH + NAD+
NADP+ + NADH
-
-
-
-
r
NADPH + NAD+
NADP+ + NADH
-
-
-
-
?
NADPH + NAD+
NADP+ + NADH
-
-
-
-
r
NADPH + NAD+
NADP+ + NADH
-
-
-
-
r
NADPH + NAD+
NADP+ + NADH
-
-
-
-
?
NADPH + NAD+
NADP+ + 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
NADPH + NAD+
NADP+ + NADH
-
-
-
-
?
NADPH + NAD+
NADP+ + NADH
-
-
-
-
?
NADPH + NAD+
NADP+ + NADH
-
-
-
-
?
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
-
-
-
?
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
-
-
-
-
?
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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2',5'-ADP
-
bacteriorhodopsin co-reconstituted enzyme, 36.8% inhibition of thio-NADP+ reduction by NADH in the dark, 34.4% in the light
2,2'-dithiodipyridine
-
0.2 mM, 45% inhibition
2,2'-thiodiethanethiole
-
0.5 mM, 37% inhibition
2,4-dinitrophenyl-3'-dephospho-CoA
-
competitive vs. NAD+, non-competitive vs. NADPH
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
34% residual activity at 1 mM
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
5,5'-dithiobis(2-nitrobenzoate)
acetyl-dephospho-CoA
-
competitive vs. NAD(H)
acetylpyridine adenine dinucleotide
-
-
cardiolipin
-
noncompetitive vs. NAD+ and NADPH
Dansyl chloride
-
0.25 mM, almost complete inactivation after 8 min, NADP+ or NADPH accelerate inhibition rate
dephospho-CoA
-
competitive vs. NAD(H)
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
formamide disulfide dihydrochloride
-
0.2 mM, 43% inhibition
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
La3+
-
0.1 mM, 50% inhibition at pH 7.0, maximal inhibition at pH 8.0
methylmethane thiosulfonate
N,N'-dicyclohexylcarbodiimide
-
0.3 mM significantly inhibits the the energy-linked NADH-NADP+ reactions, but not the nonenergy-linked NADH-NADP+ transhydrogenation
N,N'-Dicylclohexylcarbodiimide
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
N-(Ethoxycarbonyl)-2-ethoxy-1,2-dihydroquinoline
Na+
-
200 mM, 50% inhibition at pH 7.9, 300 mM, 40% inhibition at pH 5.5, 95% at pH 8.5
p-Chlororomercuriphenyl sulfonate
-
-
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
Phospholipase A
-
74% inhibition of activity in submitochondrial particles
-
Phospholipase C
-
10-20% inhibition of activity in submitochondrial particles
-
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
reduced acetylpyridine adenine dinucleotide
-
competitive vs. oxidized acetylpyridine dinucleotide, noncompetitive vs. NADPH
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+
S-nitrosoglutathione
100% inhibition at 3 mM or higher concentration
Sr2+
-
25 mM, 50% inhibition at pH 7.0
Tl+
-
20 mM, 50% inhibition at pH 7.9
additional information
-
NNT expression is 2.8fold downregulated in the vastus lateralis muscle of calorie restricted rhesus monkeys
-
2'-AMP
-
-
2'-AMP
-
noncompetitive vs. NAD+, competitive vs. NADPH
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. NAD+, noncompetitive vs. NADPH
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
Ca2+
-
-
Ca2+
-
20 mM, 50% inhibition at pH 7.0, maximal inhibition at pH 9.0
CoA
-
-
CoA
-
competitive vs. NAD(P)H
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
-
modification of Cys-893
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+
-
-
Mg2+
-
20 mM, 50% inhibition at pH 7.0, competitive vs. NADPH and thio-NADP+, noncompetitive vs. acetylpyridine adenine dinucleotide and NADH
Mg2+
-
5 mM, aprrox. 20% inhibition, 20 mM, approx. 60% inhibition
Mg2+
-
1 mM, half-maximal inhibition, 10 mM, 80% inhibition
Mn2+
-
-
Mn2+
-
10 mM, 50% inhibition at pH 7.0, maximal inhibition at pH 9.0
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
-
-
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
-
-
N,N'-Dicylclohexylcarbodiimide
-
NAD+ and acetylpyridine adenine dinucleotide protect, NADP+ accelerates inhibition
N,N'-Dicylclohexylcarbodiimide
-
-
N-(Ethoxycarbonyl)-2-ethoxy-1,2-dihydroquinoline
-
-
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
-
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
NAD+
-
product inhibition of forward reaction i.e. reduction of NADP+ by NADH
NADH
-
competitive vs. NAD+, noncompetitive vs. NADPH
NADH
-
product inhibition of reverse reaction i.e. reduction of NAD+ by NADPH
NADP+
-
noncompetitive vs. NAD+, competitive vs. NADPH
NADP+
-
product inhibition of reverse reaction i.e. reduction of NAD+ by NADPH
NADPH
-
-
NADPH
-
bacteriorhodopsin co-reconstituted enzyme, 76.9% inhibition of thio-NADP+ reduction by NADH in the dark, 57.4% in the light
NADPH
-
product inhibition of forward reaction i.e. reduction of NADP+ by NADH
p-chloromercuribenzoate
-
0.003 mM, 25% inhibition
p-chloromercuribenzoate
-
-
palmitoyl-CoA
-
-
palmitoyl-CoA
-
competitive inhibition vs. NADPH
palmitoyl-CoA
-
competitive vs. NADPH
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
triiodothyronine
-
-
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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
-
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
-
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
-
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
-
enzyme inhibition decreases NADPH levels, decreases thioredoxin and thioredoxin reductase activity, and increases toxicity to oxidative stress
malfunction
-
enzyme knockdown decreases reductive carboxylation and stimulates glucose catabolism in the tricarboxylic acid cycle
malfunction
-
gene disruption of pntA results in phenotypic growth defects observed under low light intensities in the presence of glucose, whereas under autotrophic conditions the mutant does not differ from the wild type strain
malfunction
-
lack of enzyme activity impairs peroxide metabolism in intact mitochondria
malfunction
-
the absence of enzyme leads to variation in mitochondrial function and contributes to a unique mitochondrial redox phenotype that influences susceptibility to hypertension by contributing to endothelial and vascular dysfunction
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
-
the absence of enzyme leads to variation in mitochondrial function and contributes to a unique mitochondrial redox phenotype that influences susceptibility to hypertension by contributing to endothelial and vascular dysfunction
-
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
-
metabolism
the enzyme uses energy from the mitochondrial proton gradient to produce high concentrations of NADPH
metabolism
-
the enzyme coordinates glutamine and glucose metabolism in the tricarboxylic acid cycle
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
-
mitochondrial transhydrogenation serves as a source for this NADPH. It plays a key role in larvalpupal development
physiological function
-
nicotinamide nucleotide transhydrogenase is a mitochondrial enzyme that transfers reducing equivalents from NADH to NADPH
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
the enzyme plays a role in reactive oxygen species detoxification in human adrenal glands
physiological function
-
the enzyme activity impacts mitochondrial redox balance and the development of hypertension in mice
physiological function
-
the enzyme activity in Synechocystis is directly linked to mixotrophic growth, implicating that under these conditions the enzyme functions to balance the NADH:NADPH equilibrium specifically in the direction of NADPH
physiological function
-
the enzyme links mitochondrial respiration and antioxidant activity in brain mitochondria
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
-
the enzyme activity impacts mitochondrial redox balance and the development of hypertension in mice
-
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, 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
-
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monomer
-
solution of isolated dIII domains
trimer
-
trimers of dI2dIII1 are formes in mixed solutions containing dI and dIII domains
?
-
x * 6784, soluble component, amino acid analysis
?
-
x * 54000, immunoblot with antibodies against beef heart enzyme
?
-
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
?
-
x * 56000, alpha-subunit, SDS-PAGE
dimer
-
-
dimer
-
2 * 120000, SDS-PAGE
dimer
-
x * 97000, SDS-PAGE
dimer
-
2 * 110000, SDS-PAGE
dimer
-
2 * 115000, SDS-PAGE
dimer
-
2 * 109212, calculated from cDNA sequence
dimer
-
signal peptide MW 4816, sequence of mRNA
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 * 66000, SDS-PAGE
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
two monomers with dI, dII, and dIII domain structure
dimer
-
2 * 110000, SDS-PAGE
dimer
-
2 * 111500, SDS-PAGE
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
dimer
-
two monomers with dI, dII, and dIII domain structure
tetramer
-
-
tetramer
-
alpha2,beta2, 2 * 53906 + 2 * 48667, calculation from nucleotide sequence
tetramer
-
alpha2,beta2, 2 * 50000 + 2 * 47000
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A1008P
the mutation is associated with familial glucocorticoid deficiency
A533V
the mutation is associated with familial glucocorticoid deficiency
A553V
the mutation is associated with familial glucocorticoid deficiency
D277Y
the mutation is associated with left ventricular noncompaction
G664R
the mutation is associated with familial glucocorticoid deficiency
G678A
the mutation is associated with familial glucocorticoid deficiency
G678R
the mutation is associated with familial glucocorticoid deficiency
G862D
the mutation is associated with familial glucocorticoid deficiency
H365P
the mutation is associated with familial glucocorticoid deficiency
L977P
the mutation is associated with familial glucocorticoid deficiency
N1009K
the mutation is associated with familial glucocorticoid deficiency
P437L
the mutation is associated with familial glucocorticoid deficiency
T357A
the mutation is associated with familial glucocorticoid deficiency
Y201K
the mutation is associated with familial glucocorticoid deficiency
Y388S
the mutation is associated with familial glucocorticoid deficiency
E155W
-
dIII domain, displays similar catalytic properties as wild type, introduced tryptophan fluorescence is sensitive to the redox state of the bound nucleotide
F215S
the mutant shows 31% of wild type activity
F215S
the mutation is associated with familial glucocorticoid deficiency
G200S
-
the mutation is associated with familial glucocorticoid deficiency
G200S
the mutation is associated with combined mineralocorticoid and glucocorticoid deficiency
S193N
the mutation is associated with familial glucocorticoid deficiency
S193N
the mutation is associated with FGD
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
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
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
-
enzyme deficient mutants created by insertions at condon 474, 128, and 285 of ptnA
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
-
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
-
siRNA silencing or knockdown of NNT
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