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NAD(P)H + 2,6-dichlorophenolindophenol
NAD(P)+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
NAD(P)H + K4Fe(CN)6
NAD(P)+ + K3Fe(CN)6
-
-
-
?
NADH + 2'-NADP+
NAD+ + 2'-NADPH
-
-
-
?
NADH + 3'-NADP+
NAD+ + 3'-NADPH
-
-
-
?
NADH + NADP+
NADPH + NAD+
-
-
-
?
NADH + thio-NAD+
NAD+ + thio-NADH
-
-
-
?
NADH + thio-NADP+
NAD+ + thio-NADPH
NADP+ + NADH
NADPH + NAD+
NADPH + 3-acetylpyridine-NAD+
NADP+ + 3-acetylpyridine-NADH
NADPH + deamino-NAD+
NADP+ + deamino-NADH
NADPH + NAD+
NADP+ + NADH
NADPH + pyridine aldehyde-NAD+
NADP+ + pyridine aldehyde-NADH
NADPH + thio-NAD+ + H+[side 1]
NADP+ + thio-NADH + H+[side 2]
NADPH + thio-NADP+ + H+[side 1]
NADP+ + thio-NADPH + H+[side 2]
NADH + thio-NADP+

NAD+ + thio-NADPH
-
-
-
?
NADH + thio-NADP+
NAD+ + thio-NADPH
-
-
-
-
r
NADH + thio-NADP+
NAD+ + thio-NADPH
-
-
-
-
r
NADP+ + NADH

NADPH + NAD+
Azotobacter agilis
-
degree of reversibility depends on source of enzyme
-
r
NADP+ + NADH
NADPH + NAD+
-
degree of reversibility depends on source of enzyme
-
r
NADP+ + NADH
NADPH + NAD+
-
-
-
-
NADP+ + NADH
NADPH + NAD+
-
-
-
r
NADP+ + NADH
NADPH + NAD+
-
diaphorase-type reactions with NAD(P)H, K3Fe(CN)6 and 2,6-dichlorophenol indophenol
-
-
NADP+ + NADH
NADPH + NAD+
Chromatium sp.
-
poorly reversible
-
-
r
NADP+ + NADH
NADPH + NAD+
-
-
-
-
r
NADP+ + NADH
NADPH + NAD+
-
-
-
-
r
NADP+ + NADH
NADPH + NAD+
-
4B-specific for NAD(P)H
-
-
?
NADP+ + NADH
NADPH + NAD+
-
-
-
r
NADP+ + NADH
NADPH + NAD+
-
4B-specific for NAD(P)H
-
-
NADP+ + NADH
NADPH + NAD+
-
reduction of NADP+ is preferred
-
r
NADP+ + NADH
NADPH + NAD+
-
diaphorase-type reactions with NAD(P)H, K3Fe(CN)6 and 2,6-dichlorophenol indophenol
-
-
NADP+ + NADH
NADPH + NAD+
-
-
-
-
-
NADP+ + NADH
NADPH + NAD+
-
degree of reversibility depends on source of enzyme
-
r
NADP+ + NADH
NADPH + NAD+
-
4B-specific for NAD(P)H
-
-
?
NADP+ + NADH
NADPH + NAD+
-
reduction of NADP+ is preferred
-
r
NADPH + 3-acetylpyridine-NAD+

NADP+ + 3-acetylpyridine-NADH
-
-
-
?
NADPH + 3-acetylpyridine-NAD+
NADP+ + 3-acetylpyridine-NADH
-
-
-
?
NADPH + 3-acetylpyridine-NAD+
NADP+ + 3-acetylpyridine-NADH
-
-
-
?
NADPH + deamino-NAD+

NADP+ + deamino-NADH
-
-
-
?
NADPH + deamino-NAD+
NADP+ + deamino-NADH
-
-
-
?
NADPH + deamino-NAD+
NADP+ + deamino-NADH
-
-
-
?
NADPH + deamino-NAD+
NADP+ + deamino-NADH
-
-
-
?
NADPH + deamino-NAD+
NADP+ + deamino-NADH
-
-
-
?
NADPH + NAD+

NADP+ + NADH
-
-
-
-
?
NADPH + NAD+
NADP+ + NADH
-
-
-
?
NADPH + NAD+
NADP+ + NADH
-
-
-
r
NADPH + NAD+
NADP+ + NADH
-
-
-
-
?
NADPH + NAD+
NADP+ + NADH
-
-
-
-
?
NADPH + pyridine aldehyde-NAD+

NADP+ + pyridine aldehyde-NADH
-
-
-
?
NADPH + pyridine aldehyde-NAD+
NADP+ + pyridine aldehyde-NADH
-
-
-
?
NADPH + pyridine aldehyde-NAD+
NADP+ + pyridine aldehyde-NADH
-
-
-
?
NADPH + thio-NAD+ + H+[side 1]

NADP+ + thio-NADH + H+[side 2]
-
-
-
?
NADPH + thio-NAD+ + H+[side 1]
NADP+ + thio-NADH + H+[side 2]
-
-
-
r
NADPH + thio-NAD+ + H+[side 1]
NADP+ + thio-NADH + H+[side 2]
EcSTH has a 1.25fold preference for NADPH over thio-NAD+
-
-
r
NADPH + thio-NADP+ + H+[side 1]

NADP+ + thio-NADPH + H+[side 2]
-
-
-
?
NADPH + thio-NADP+ + H+[side 1]
NADP+ + thio-NADPH + H+[side 2]
-
-
-
?
NADPH + thio-NADP+ + H+[side 1]
NADP+ + thio-NADPH + H+[side 2]
-
-
-
?
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5'-AMP
-
5 mM, 92% inhibition of NADP+ reduction, complete inhibition of NAD+ reduction
ADP
-
5 mM, 94% inhibition of NADP+ reduction, complete inhibition of NAD+ reduction
arsenate
-
complete inhibition of activity in either direction
ATP
-
5 mM, 81% inhibition of NADP+ reduction, complete inhibition of NAD+ reduction
beta-mercaptoethanol
72% residual activity at 0.2% (v/v)
Ca2+
91.2% residual activity at 2 mM; slightly inhibitory
CTP
-
5 mM, 86% inhibition of NADP+ reduction
Cu2+
; complete inhibition at 2 mM
diphosphate
-
5 mM, 91% inhibition of NADP+ reduction
dithiothreitol
75.3% residual activity at 2 mM
EDTA
; 72.6% residual activity at 2 mM
GTP
-
5 mM, 89% inhibition of NADP+ reduction
Mn2+
; 67% residual activity at 2 mM
NAD+
-
competitive to thio-NAD+, uncompetitive with respect to NADPH
NADPH
EcSTH activity is strongly inhibited by excess NADPH, but not by thio-NAD+; the enzyme is strongly inhibited by excess NADPH
Ni2+
; 7.4% residual activity at 2 mM
p-Aminophenylarsenoxide
-
0.1 mM, 40-60% inhibition in the absence of either phosphate or magnesium ions, reduction of NAD+ by NADPH in cell-free extracts is rapidly and completely inhibited in the presence of 20 mM phosphate
p-chloromercuribenzoate
-
0.044 mM, 40-50% inhibition after 30 min, activity can be restored by adding 2-mercaptoethanol
phosphoenolpyruvate
-
87% inhibition of NADP+ reduction
pyridoxal 5'-phosphate
-
5 mM, 91% inhibition of NADP+ reduction
TTP
-
2 mM, 71% inhibition of NADP+ reduction
Zn2+
; 10.1% residual activity at 2 mM
2'-AMP

Chromatium sp.
-
-
NADP+

-
uncompetitive to thio-NAD+
NADP+
-
0.01 mM, 28% inhibition of NAD+ reduction with NADPH, 12.5% inhibition of NADP+ reduction with NADPH; inhibition of 2'-AMP activated reaction
NADP+
-
inhibition in absence of Ca2+; strong inhibition in the absence of Ca2+, saturation with Ca2+ completely abolishes inhibition
p-hydroxymercuribenzoate

-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
dependent on presence of oxidized or reduced substrate
phosphate

-
10-25 mM, 60-70% inhibition of purified enzyme, complete inhibition of enzyme in cell-free extracts by 5-10 mM phosphate, NADP+ reduction by NADH is inhibited, reduction of NAD+ by NADPH is hardly affected
phosphate
-
5 mM, complete inhibition of activity in either direction
additional information

no or poor inhibition of the enzyme by Na+, Rb+, K+, Li+,, and Mg2+; the enzyme is not inhibited by thio-NAD+ and DMSO
-
additional information
-
not inhibited by palmitoyl-CoA, not affected by treatment with 0.2 mg trypsin/mg protein
-
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4 - 50
the enzyme retains 50% activity after 5 h at 50°C. The enzyme is stable at 4°C for 25 days and retains 65% activity at 25°C. The enzyme is rapidly inactivated at high temperatures, retaining 80%, 50% and 10% activity after incubation for 30 min at 50, 57 and 62°C, respectively
51
-
25 min, 50% inactivation, accelerated by addition of NADPH, reactivation by FAD
55
-
approx. 50% activity lost after about 2 min, almost complete loss of activity after 20 min, biphasic inactivation: 70% activity lost with a first-order inactivation constant, 30% is lost much more rapidly, rate of thermal inactivation depends on concentration of NAD+, NADP+, NADH, NADPH, free FAD, Mg2+ and phosphate, independent of pH between pH 5 and pH 9, significant acceleration outside this range, addition of 1 mM FAD lowers inactivation rate about 20fold
57
purified enzyme, pH 7.5, 30 min, 50% activity remaining
62
purified enzyme, pH 7.5, 30 min, 10% activity remaining
65
-
15 min, complete inactivation, protection by FAD
50

-
1 h stable, inactivation is dramatically accelerated by NADH and NADPH, partial protection by NADP+ and FMN, almost full protection by FAD
50
purified enzyme, pH 7.5, 5h, 50% activity remaining, 80% activity remaining after 30 min
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Adenoma
Pancreatic islet expression profiling in diabetes-prone C57BLKS/J mice reveals transcriptional differences contributed by DBA loci, including Plagl1 and Nnt.
Adrenal Insufficiency
Association of adrenal insufficiency with insulin-dependent diabetes mellitus in a patient with inactivating mutations in nicotinamide nucleotide transhydrogenase: a phenocopy of the animal model.
Adrenal Rest Tumor
Combined adrenal failure and testicular adrenal rest tumor in a patient with nicotinamide nucleotide transhydrogenase deficiency.
Atherosclerosis
Absence of Nicotinamide Nucleotide Transhydrogenase in C57BL/6J Mice Exacerbates Experimental Atherosclerosis.
Bacteremia
Acinetobacter baumannii Genes Required for Bacterial Survival during Bloodstream Infection.
Carcinoma, Hepatocellular
Pyridine-adenine dinucleotide transhydrogenase activity in cells cultured from rat hepatoma.
Cystinosis
Enzymic reduction of cystine and glutathione in cultivated human fibroblast from normal subjects and patients with cystinosis.
Diabetes Mellitus, Type 1
Association of adrenal insufficiency with insulin-dependent diabetes mellitus in a patient with inactivating mutations in nicotinamide nucleotide transhydrogenase: a phenocopy of the animal model.
Glucose Intolerance
A High-Throughput Assay for Modulators of NNT Activity in Permeabilized Yeast Cells.
Glucose Intolerance
Defective insulin secretory response to intravenous glucose in C57Bl/6J compared to C57Bl/6N mice.
Glucose Intolerance
Deletion of nicotinamide nucleotide transhydrogenase: a new quantitive trait locus accounting for glucose intolerance in C57BL/6J mice.
Glucose Intolerance
Dysregulation of glucose homeostasis in nicotinamide nucleotide transhydrogenase knockout mice is independent of uncoupling protein 2.
Glucose Intolerance
K(ATP) channels and insulin secretion: a key role in health and disease.
Glucose Intolerance
Mitochondrial transhydrogenase--a key enzyme in insulin secretion and, potentially, diabetes.
Glucose Intolerance
Nicotinamide nucleotide transhydrogenase mRNA expression is related to human obesity.
Glucose Intolerance
Obesity and Type 2 Diabetes: Slow Down! - Can Metabolic Deceleration Protect The Islet Beta Cell From Excess Nutrient-Induced Damage?
Heart Failure
Mitochondrial Bioenergetics and Dysfunction in Failing Heart.
Hypertension
Nicotinamide nucleotide transhydrogenase activity impacts mitochondrial redox balance and the development of hypertension in mice.
Infection
Acinetobacter baumannii Genes Required for Bacterial Survival during Bloodstream Infection.
Liver Neoplasms, Experimental
Comparison of transhydrogenase and pyridine nucleotide-cytochrome c reductase activities in rat liver and Novikoff hepatoma.
Metabolic Diseases
A Direct Comparison of Metabolic Responses to High Fat Diet in C57BL/6J and C57BL/6NJ Mice.
nad(p)+ transhydrogenase (si-specific) deficiency
Combined adrenal failure and testicular adrenal rest tumor in a patient with nicotinamide nucleotide transhydrogenase deficiency.
Neoplasms
Combined adrenal failure and testicular adrenal rest tumor in a patient with nicotinamide nucleotide transhydrogenase deficiency.
Neoplasms
Mammalian NADH:ubiquinone oxidoreductase (Complex I) and nicotinamide nucleotide transhydrogenase (Nnt) together regulate the mitochondrial production of H?O?--implications for their role in disease, especially cancer.
Neoplasms
Studies on the isocitrate dehydrogenase. II. Isocitrate dehydrogenase and transhydrogenase in tumor bearing rat liver and ascites tumor cells.
Neoplasms
[Occurrence of pyridine nucleotide transhydrogenase in mitochondria of various ascites tumors]
Obesity
Adipose tissue metabolism and inflammation are differently affected by weight loss in obese mice due to either a high-fat diet restriction or change to a low-fat diet.
Obesity
Alterations of Pancreatic Islet Structure, Metabolism and Gene Expression in Diet-Induced Obese C57BL/6J Mice.
Obesity
Diet-induced Obesity in Two C57BL/6 Substrains With Intact or Mutant Nicotinamide Nucleotide Transhydrogenase (Nnt) Gene.
Obesity
Nicotinamide nucleotide transhydrogenase mRNA expression is related to human obesity.
Obesity
Obesity and Type 2 Diabetes: Slow Down! - Can Metabolic Deceleration Protect The Islet Beta Cell From Excess Nutrient-Induced Damage?
Pneumonia
Evidence for a nicotinamide nucleotide transhydrogenase in Klebsiella pneumoniae.
Tics
Upregulation of mitochondrial NAD(+) levels impairs the clonogenicity of SSEA1(+) glioblastoma tumor-initiating cells.
Tuberculosis
A hybrid of the transhydrogenases from Rhodospirillum rubrum and Mycobacterium tuberculosis catalyses rapid hydride transfer but not the complete, proton-translocating reaction.
Tuberculosis
Isolation of a 43 kDa protein from Mycobacterium tuberculosis H37Rv and its identification as a pyridine nucleotide transhydrogenase.
Tuberculosis
Membrane and membrane-associated proteins in Triton X-114 extracts of Mycobacterium bovis BCG identified using a combination of gel-based and gel-free fractionation strategies.
Tuberculosis
Similarities between alanine dehydrogenase and the N-terminal part of pyridine nucleotide transhydrogenase and their possible implication in the virulence mechanism of Mycobacterium tuberculosis.
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Voordouw, G.; van der Vies, S.M.; Themmen, A.P.N.
Why are two different types of pyridine nucleotide transhydrogenase found in living organisms?
Eur. J. Biochem.
131
527-533
1983
Azotobacter vinelandii, Pseudomonas aeruginosa, Pseudomonas fluorescens
brenda
Voordouw, G.; de Haard, H.; Timmermans, J.A.M.; Veeger, C.; Zabel, P.
Dissociation and assembly of pyridine nucleotide transhydrogenase from Azotobacter vinelandii
Eur. J. Biochem.
127
267-274
1982
Azotobacter vinelandii
brenda
Voordouw, G.; van der Vies, S.M.; Eweg, J.K.; Veeger, C.; van Breemen, J.F.L.; van Bruggen, E.F.J.
Pyridine nucleotide transhydrogenase from Azotobacter vinelandii. Improved purification, physical properties and subunit arrangement in purified polymers
Eur. J. Biochem.
111
347-355
1980
Azotobacter vinelandii
brenda
Voordouw, G.; van der Vies, S.; Scholten, J.W.; Veeger, C.
Pyridine nucleotide transhydrogenase from Azotobacter vinelandii. Differences in properties between the purified and the cell-free extract enzyme
Eur. J. Biochem.
107
337-344
1980
Azotobacter vinelandii
brenda
Voordouw, G.; Veeger, C.; van Breemen, J.F.L.; van Bruggen, E.F.J.
Structure of pyridine nucleotide transhydrogenase from Azotobacter vinelandii
Eur. J. Biochem.
98
447-454
1979
Azotobacter vinelandii
brenda
Höjeberg, B.; Rydström, J.
Ca2+-dependent allosteric regulation of nicotinamide nucleotide transhydrogenase from Pseudomonas aeruginosa
Eur. J. Biochem.
77
235-241
1977
Pseudomonas aeruginosa
brenda
Collins, P.A.; Knowles, C.J.
Transhydrogenase activity in the marine bacterium Beneckea natriegens
Biochim. Biophys. Acta
480
77-82
1977
Vibrio natriegens
brenda
Widmer, F.; Kaplan, N.O.
Regulatory properties of the pyridine nucleotide transhydrogenase from Pseudomonas aeruginosa. Kinetic studies and fluorescence titration
Biochemistry
15
4693-4699
1976
Pseudomonas aeruginosa
brenda
Wermuth, B.; Kaplan, N.O.
Pyridine nucleotide transhydrogenase from Pseudomonas aeruginosa: purification by affinity chromatography and physicochemical properties
Arch. Biochem. Biophys.
176
136-143
1976
Pseudomonas aeruginosa
brenda
Hoek, J.B.; Rydström, J.; Höjeberg, B.
Comparative studies on nicotinamide nucleotide transhydrogenase from different sources
Biochim. Biophys. Acta
333
237-245
1974
Pseudomonas aeruginosa
brenda
Rydström, J.; Hoek, J.B.; Höjeberg, B.
Ca 2+ -dependent allosteric regulation of nicotinamide nucleotide transhydrogenase from Pseudomonas aeruginosa
Biochem. Biophys. Res. Commun.
52
421-429
1973
Pseudomonas aeruginosa
brenda
Middleditch, L.E.; Atchison, R.W.; Chung, A.E.
Pyridine nucleotide transhydrogenase from Azotobacter vinelandii. Some aspects of its structure
J. Biol. Chem.
247
6802-6809
1972
Azotobacter vinelandii
brenda
Van den Broek, H.W.J.; Santema, J.S.; Wassink, J.H.; Veeger, C.
Pyridine-nucleotide transhydrogenase. 1. Isolation, purification and characterisation of the transhydrogenase from Azotobacter vinelandii
Eur. J. Biochem.
24
31-45
1971
Azotobacter vinelandii
brenda
Van den Broek, H.W.J.; van Breemen, J.F.L.; van Bruggen, E.F.J.; Veeger, C.
Pyridine-nucleotide transhydrogenase. 2. Electron-microscopic studies on the transhydrogenase from Azotobacter vinelandii
Eur. J. Biochem.
24
46-54
1971
Azotobacter vinelandii
brenda
Van den Broek, H.W.J.; Veeger, C.
Pyridine-nucleotide transhydrogenase. 5. Kinetic studies on transhydrogenase from Azotobacter vinelandii
Eur. J. Biochem.
24
72-82
1971
Azotobacter vinelandii
brenda
Cohen, P.T.; Kaplan, N.O.
Kinetic characteristics of the pyridine nucleotide transhydrogenase from Pseudomonas aeruginosa
J. Biol. Chem.
245
4666-4672
1970
Pseudomonas aeruginosa
brenda
Cohen, P.T.; Kaplan, N.O.
Purification and properties of the pyridine nucleotide transhydrogenase from Pseudomonas aeruginosa
J. Biol. Chem.
245
2825-2836
1970
Pseudomonas aeruginosa
brenda
Chung, A.E.
Pyridine nucleotide transhydrogenase from Azotobacter vinelandii
J. Bacteriol.
102
438-447
1970
Azotobacter vinelandii
brenda
French, C.E.; Boonstra, B.; Bufton, K.A.; Bruce, N.C.
Cloning, sequence, and properties of the soluble pyridine nucleotide transhydrogenase of Pseudomonas fluorescens
J. Bacteriol.
179
2761-2765
1997
Pseudomonas fluorescens
brenda
Bykova, N.V.; Rasmusson, A.G.; Igamberdiev, A.U.; Gardestrom, P.; Moller, I.M.
Two separate transhydrogenase activities are present in plant mitochondria
Biochem. Biophys. Res. Commun.
265
106-111
1999
Pisum sativum, Solanum tuberosum
brenda
Rydström, J.; Hoek, J.B.; Ernster, L.
Nicotinamide nucleotide transhydrogenases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
13
51-88
1976
Azotobacter agilis, Azotobacter chroococcum, Azotobacter vinelandii, Chromatium sp., Pseudomonas aeruginosa, Pseudomonas fluorescens
-
brenda
Ichinose, H.; Kamiya, N.; Goto, M.
Enzymatic redox cofactor regeneration in organic media: functionalization and application of glycerol dehydrogenase and soluble transhydrogenase in reverse micelles
Biotechnol. Prog.
21
1192-1197
2005
Escherichia coli
brenda
Sanchez, A.M.; Andrews, J.; Hussein, I.; Bennett, G.N.; San, K.Y.
Effect of overexpression of a soluble pyridine nucleotide transhydrogenase (UdhA) on the production of poly(3-hydroxybutyrate) in Escherichia coli
Biotechnol. Prog.
22
420-425
2006
Escherichia coli
brenda
Mouri, T.; Shimizu, T.; Kamiya, N.; Goto, M.; Ichinose, H.
Design of a cytochrome P450BM3 reaction system linked by two-step cofactor regeneration catalyzed by a soluble transhydrogenase and glycerol dehydrogenase
Biotechnol. Prog.
25
1372-1378
2009
Escherichia coli
brenda
Cao, Z.; Song, P.; Xu, Q.; Su, R.; Zhu, G.
Overexpression and biochemical characterization of soluble pyridine nucleotide transhydrogenase from Escherichia coli
FEMS Microbiol. Lett.
320
9-14
2011
Escherichia coli, Escherichia coli (P27306)
brenda
Jan, J.; Martinez, I.; Wang, Y.; Bennett, G.; San, K.
Metabolic engineering and transhydrogenase effects on NADPH availability in Escherichia coli
Biotechnol. Prog.
29
1124-1130
2013
Escherichia coli, Escherichia coli (P27306)
brenda
Yamaguchi, R.; Kato, F.; Hasegawa, T.; Katsumata, N.; Fukami, M.; Matsui, T.; Nagasaki, K.; Ogata, T.
A novel homozygous mutation of the nicotinamide nucleotide transhydrogenase gene in a Japanese patient with familial glucocorticoid deficiency
Endocr. J.
60
855-859
2013
Homo sapiens
brenda
Haverkorn van Rijsewijk, B.R.; Kochanowski, K.; Heinemann, M.; Sauer, U.
Distinct transcriptional regulation of the two Escherichia coli transhydrogenases PntAB and UdhA
Microbiology
162
1672-1679
2016
Escherichia coli, Escherichia coli BW25113
brenda