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Information on EC 1.6.1.2 - NAD(P)+ transhydrogenase (Re/Si-specific) and Organism(s) Bos taurus
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1.6.1.2 NAD(P)+ transhydrogenase (Re/Si-specific)IUBMB Comments
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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Word Map
- 1.6.1.2
- nadp+
- rhodospirillum
- rubrum
-
hydride
-
transhydrogenation
-
nadh-binding
-
submitochondrial
-
chromatophores
- acetylpyridine
-
dihydronicotinamide
- isobutanol
- thio-nadp+
-
acpdad+
The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
pntab, energy-linked transhydrogenase, mitochondrial transhydrogenase, proton-translocating transhydrogenase, proton-translocating nicotinamide nucleotide transhydrogenase, nadph transhydrogenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dII
-
-
-
-
dIII
-
-
-
-
energy-linked transhydrogenase
-
-
-
-
H+-thase
-
-
-
-
NAD transhydrogenase
-
-
-
-
NAD(P) transhydrogenase
-
-
-
-
NADH transhydrogenase
-
-
-
-
NADH-NADP-transhydrogenase
-
-
-
-
NADPH-NAD oxidoreductase
-
-
-
-
NADPH-NAD transhydrogenase
-
-
-
-
NADPH:NAD+ transhydrogenase
-
-
-
-
nicotinamide adenine dinucleotide (phosphate) transhydrogenase
-
-
-
-
nicotinamide nucleotide transhydrogenase
-
-
-
-
pyridine nucleotide transferase
-
-
-
-
pyridine nucleotide transhydrogenase
-
-
-
-
transhydrogenase
-
-
-
-
transhydrogenase, nicotinamide adenine dinucleotide (phosphate)
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
enzyme is stereospecific for the 4A hydrogen of NADH and the 4B hydrogen of NADPH
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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)].
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
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
NADPH + oxidized 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
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+
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
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
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NADH + NADP+
NAD+ + NADPH
-
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+
-
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
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
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
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
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,4-dinitrophenyl-3'-dephospho-CoA
-
competitive vs. NAD+, non-competitive vs. NADPH
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
-
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 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-(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-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
Na+
-
200 mM, 50% inhibition at pH 7.9, 300 mM, 40% inhibition at pH 5.5, 95% at pH 8.5
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
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
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+
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
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-(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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
14.2
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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, 742520
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospholipoprotein
-
5 mol loosely bound phospholipids, 9 mol tightly bound phospholipids
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
cations prevent from tryptic inactivation, 95% protection with Mn2+, 89% with Ca2+ and 79% with Mg2+
-
unstable, loses 30-50% activity within 48 h at 4Ā°C, remainder of the enzyme becomes inactive after 2 weeks, complete inactivation after freezing at -20Ā°C or -70Ā°C overnight, enzyme is very susceptible to trypsinolysis, NADH protects from tryptic inactivation, NADPH promotes tryptic inactivation
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acetone
-
used for conversion of mitochondria to an acetone powder causes inactivation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4Ā°C, 0.1 M sodium phosphate buffer, pH 7.5, 1 mM dithiothreitol, 0.05% sodium cholate
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rydström, J.; Hoek, J.B.; Ernster, L.
Nicotinamide nucleotide transhydrogenases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
13
51-88
1976
Bos taurus, Mammalia
-
Yamaguchi, M.; Hatefi, Y.
Mitochondrial energy-linked nicotinamide nucleotide transhydrogenase. Membrane topography of the bovine enzyme
J. Biol. Chem.
266
5728-5735
1991
Bos taurus
Yamaguchi, M.; Hatefi, Y.
Mitochondrial nicotinamide nucleotide transhydrogenase: NADPH binding increases and NADP binding decreases the acidity and susceptibility to modification of cysteine-893
Biochemistry
28
6050-6056
1989
Bos taurus
Yamaguchi, M.; Hatefi, Y.; Trach, K.; Hoch, J.A.
Amino acid sequence of the signal peptide of mitochondrial nicotinamide nucleotide transhydrogenase as determined from the sequence of its messenger RNA
Biochem. Biophys. Res. Commun.
157
24-29
1988
Bos taurus
Yamaguchi, M.; Hatefi, Y.; Trach, K.; Hoch, J.A.
The primary structure of the mitochondrial energy-linked nicotinamide nucleotide transhydrogenase deduced from the sequence of cDNA clones
J. Biol. Chem.
263
2761-2767
1988
Bos taurus
Persson, B.; Ahnström, G.; Rydström, J.
Energy-linked nicotinamide nucleotide transhydrogenase: hydrodynamic properties and active form of purified and membrane-bound mitochondrial transhydrogenase from beef heart
Arch. Biochem. Biophys.
259
341-349
1987
Bos taurus
Eytan, G.D.; Eytan, E.; Rydström, J.
Energy-linked nicotinamide-nucleotide transhydrogenase. Light-driven transhydrogenase catalyzed by transhydrogenase from beef heart mitochondria reconstituted with bacteriorhodopsin
J. Biol. Chem.
262
5015-5019
1987
Bos taurus
Eytan, G.D.; Persson, B.; Ekebacke, A.; Rydström, J.
Energy-linked nicotinamide-nucleotide transhydrogenase. Characterization of reconstituted ATP-driven transhydrogenase from beef heart mitochondria
J. Biol. Chem.
262
5008-5014
1987
Bos taurus
Persson, B.; Rydström, J.
Evidence for a role of a vicinal dithiol in catalysis and proton pumping in mitochondrial nicotinamide nucleotide transhydrogenase
Biochem. Biophys. Res. Commun.
142
573-578
1987
Bos taurus
Wu, L.N.Y.; Alberta, J.A.; Fisher, R.R.
Purification and reconstitution of bovine heart mitochondrial transhydrogenase
Methods Enzymol.
126
353-360
1986
Bos taurus
Yamaguchi, M.; Hatefi, Y.
Mitochondrial nicotinamide nucleotide transhydrogenase: inhibition by ethoxyformic anhydride, dansyl chloride, and pyridoxal phosphate
Arch. Biochem. Biophys.
243
20-27
1985
Bos taurus
Phelps, D.C.; Hatefi, Y.
Mitochondrial nicotinamide nucleotide transhydrogenase: nonidentical modification by N,N-dicyclohexylcarbodiimide and N-(ethoxycarbonyl)-2-ethoxy-1,2-dihydroquinoline at the NAD(H) binding site
Arch. Biochem. Biophys.
243
298-304
1985
Bos taurus
Carlenor, E.; Tang, H.L.; Rydström, J.
Affinity chromatography of mitochondrial nicotinamide nucleotide transhydrogenase
Anal. Biochem.
148
518-523
1985
Bos taurus, Rattus norvegicus
Phelps, D.C.; Hatefi, Y.
Mitochondrial nicotinamide nucleotide transhydrogenase: active site modification by 5-[p-(fluorosulfonyl)benzoyl]adenosine
Biochemistry
24
3503-3507
1985
Bos taurus
Kozlov, I.A.; Milgrom, Y.M.; Saburova, L.A.; Sobolev, A.Y.
The interaction of mitochondrial transhydrogenase with derivatives of coenzyme A
Eur. J. Biochem.
145
413-416
1984
Bos taurus
Phelps, D.C.; Hatefi, Y.
Interaction of purified nicotinamidenucleotide transhydrogenase with dicyclohexylcarbodiimide
Biochemistry
23
4475-4480
1984
Bos taurus
Persson, B.; Enander, K.; Tang, H.L.; Rydström, J.
Energy-linked nicotinamide nucleotide transhydrogenase. Properties of proton-translocating mitochondrial transhydrogenase from beef heart purified by fast protein liquid chromatography
J. Biol. Chem.
259
8626-8632
1984
Bos taurus
Pennington, R.M.; Fisher, R.R.
Reconstituted mitochondrial transhydrogenase is a transmembrane protein
FEBS Lett.
164
345-349
1983
Bos taurus
Wu, L.N.W.; Fisher, R.R.
Subunit structure of submitochondrial particle membrane transhydrogenase
J. Biol. Chem.
258
7847-7851
1983
Bos taurus
Enander, K.; Rydström, J.
Energy-linked nicotinamide nucleotide transhydrogenase. Kinetics and regulation of purified and reconstituted transhydrogenase from beef heart mitochondria
J. Biol. Chem.
257
14760-14766
1982
Bos taurus
Wu, L.N.Y.; Fisher, R.R.
Stereochemistry of NADPH leads to NADP+ transhydrogenation catalyzed by bovine heart mitochondrial pyridine dinucleotide transhydrogenase
J. Biol. Chem.
257
11680-11683
1982
Bos taurus
Wu, L.N.Y.; Pennington, R.M.; Everett, T.D.; Fisher, R.R.
An improved method for the purification of bovine heart mitochondrial transhydrogenase
J. Biol. Chem.
257
4052-4055
1982
Bos taurus
Phelps, D.C.; Hatefi, Y.
Inhibition of the mitochondrial nicotinamide nucleotide transhydrogenase by dicyclohexylcarbodiimide and diethylpyrocarbonate
J. Biol. Chem.
256
8217-8221
1981
Bos taurus
Anderson, W.M.; Fisher, R.R.
The subunit structure of bovine heart mitochondrial transhydrogenase
Biochim. Biophys. Acta
635
194-199
1981
Bos taurus
Anderson, W.M.; Fowler, W.T.; Pennington, R.M.; Fisher, R.R.
Immunochemical characterization and purification of bovine heart mitochondrial pyridine dinucleotide transhydrogenase
J. Biol. Chem.
256
1888-1895
1981
Bos taurus
Blazyk, J.F.; Blazyk, J.M.; Kline, C.M.
Temperature-dependent changes in the activity and tryptic susceptibility of membrane-bound transhydrogenase
J. Biol. Chem.
256
691-694
1981
Bos taurus
O'Neal, S.G.; Earle, S.R.; Fisher, R.R.
The effect of metal ions on mitochondrial pyridine dinucleotide transhydrogenase
Biochim. Biophys. Acta
589
217-230
1980
Bos taurus
Rydström, J.; Fleischer, S.
Reconstitution of mitochondrial nicotinamide nucleotide transhydrogenase from beef heart with synthetic phospholipids
Methods Enzymol.
55
811-816
1979
Bos taurus
Rydström, J.
Assay of nicotinamide nucleotide transhydrogenases in mammalian, bacterial, and reconstituted systems
Methods Enzymol.
55
261-273
1979
Azotobacter sp., Bos taurus, Escherichia coli, Mammalia
Höjeberg, B.; Rydström, J.
Purification of mitochondrial nicotinamide nucleotide transhydrogenase from beef heart
Methods Enzymol.
55
275-283
1979
Bos taurus
Anderson, W.M.; Fisher, R.R.
Purification and partial characterization of bovine heart mitochondrial pyridine dinucleotide transhydrogenase
Arch. Biochem. Biophys.
187
180-190
1978
Bos taurus
Höjeberg, B.; Rydström, J.
Purification and molecular properties of reconstitutively active nicotinamide nucleotide transhydrogenase from beef heart mitochondria
Biochem. Biophys. Res. Commun.
78
1183-1190
1977
Bos taurus
Rydström, J.
Energy-linked nicotinamide nucleotide transhydrogenases
Biochim. Biophys. Acta
463
155-184
1977
Bos taurus, Escherichia coli, Rattus norvegicus, Rhodospirillum rubrum
O'Neal, S.G.; Fisher, R.R.
Studies on sulfhydryl group modification of mitochondrial pyridine dinucleotide transhydrogenase
J. Biol. Chem.
252
4552-4556
1977
Bos taurus
Rydström, J.; Heok, J.B.; Ericson, B.G.; Hundal, T.
Evidence for a lipid dependence of mitochondrial nicotinamide nucleotide transhydrogenase
Biochim. Biophys. Acta
430
419-425
1976
Bos taurus
Fisher, R.R.; Kaplan, N.O.
Studies on the mitochondrial energy-linked pyridine nucleotide transhydrogenase
Biochemistry
12
1182-1188
1973
Bos taurus
Fisher, R.R.; Earle, S.R.
Membrane-bound pyridine dinucleotide transhydrogenases
The Pyridine Nucleotide Coenzymes (Everse, J. , Andersson, B. , You, K. S. , eds. ) Academic Press, New York
279-324
1982
Bos taurus, Mammalia
-
Rydström, J.; Persson, B.; Carlenor, E.
Transhydrogenases linked to pyridine nucleotides
Pyridine Nucleotide Coenzymes, Chem. Biochem. Med. Aspects (Dolphin, D. , Poulson, R. , Avramovic, O. , eds. ) Wiley and Sons, New York
2B
433-461
1987
Bos taurus, Mammalia
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Rydström, J.
Mitochondrial nicotinamide nucleotide transhydrogenase
Mitochondria and Microsomes (Lee, C. P. , Schatz, G. , Dallner, G. eds. ) Addison-Wesley, Reading MA
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1981
Bos taurus
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Kaufman, B.; Kaplan, N.O.
Pyridine nucleotide transhydrogenase. VIII. Properties of the transhydrogenase reactions of an enzyme complex isolated from beef heart mitochondria
J. Biol. Chem.
236
2133-2139
1961
Bos taurus
Yamaguchi, M.; Hatefi, Y.
Energy-transducing nicotinamide nucleotide transhydrogenase. Nucleotide binding properties of the purified enzyme and proteolytic fragments
J. Biol. Chem.
268
17871-17877
1993
Bos taurus
Bizouarn, T.; Grimley, R.; Diggle, C.; Thomas, C.M.; Jackson, J.B.
Mutations at tyrosine-235 in the mobile loop region of domain I protein of transhydrogenase from Rhodospirillum rubrum strongly inhibit hydride transfer
Biochim. Biophys. Acta
1320
265-274
1997
Bos taurus, Rhodospirillum rubrum
Bizouarn, T.; Fjellstrom, O.; Meuller, J.; Axelsson, M.; Bergkvist, A.; Johansson, C.; Goran Karlsson, B.; Rydstrom, J.
Proton translocating nicotinamide nucleotide transhydrogenase from E. coli. Mechanism of action deduced from its structural and catalytic properties
Biochim. Biophys. Acta
1457
211-228
2000
Bos taurus, Escherichia coli, Rhodospirillum rubrum
Jackson, J.B.; White, S.A.; Quirk, P.G.; Venning, J.D.
The alternating site, binding change mechanism for proton translocation by Transhydrogenase
Biochemistry
41
4173-4185
2002
Bos taurus, Escherichia coli, Entamoeba histolytica, Homo sapiens, Rhodospirillum rubrum
Jackson, J.B.; Leung, J.H.; Stout, C.D.; Schurig-Briccio, L.A.; Gennis, R.B.
Review and Hypothesis. New insights into the reaction mechanism of transhydrogenase Swivelling the dIII component may gate the proton channel
FEBS Lett.
589
2027-2033
2015
Bos taurus, Entamoeba histolytica, Thermus thermophilus, Rhodospirillum rubrum
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