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Information on EC 1.6.1.1 - NAD(P)+ transhydrogenase (Si-specific)
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1.6.1.1 NAD(P)+ transhydrogenase (Si-specific)IUBMB Comments
The enzyme from Azotobacter vinelandii is a flavoprotein (FAD). It is Si-specific with respect to both NAD+ and NADP+. Also acts on deamino coenzymes [cf. EC 1.6.1.2 NAD(P)+ transhydrogenase (Re/Si-specific)].
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Word Map
- 1.6.1.1
- nadp+
-
transhydrogenation
- rhodospirillum
-
hydride
-
proton-translocating
- rubrum
- succinate
-
submitochondrial
- pntab
- beef
-
malic
-
nadh-binding
-
proton-pumping
-
energy-dependent
-
chromatophores
- azotobacter
- vinelandii
-
energization
-
glutathione-insulin
-
acetylpyridine
-
hymenolepis
-
substrains
- dccd
- n,n'-dicyclohexylcarbodiimide
-
energy-transducing
-
cysteine-free
-
atp-driven
- diminuta
- biotechnology
The enzyme appears in viruses and cellular organisms
Synonyms
transhydrogenase, nicotinamide nucleotide transhydrogenase, pyridine nucleotide transhydrogenase, soluble transhydrogenase, soluble pyridine nucleotide transhydrogenase, nad(p) transhydrogenase, non-energy-linked transhydrogenase, nad transhydrogenase, h+-thase, nadph-nad transhydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
nicotinamide nucleotide transhydrogenase
soluble pyridine nucleotide transhydrogenase
soluble transhydrogenase
STH
UdhA
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NADPH + NAD+ = NADP+ + NADH
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
NADPH:NAD+ oxidoreductase (Si-specific)
The enzyme from Azotobacter vinelandii is a flavoprotein (FAD). It is Si-specific with respect to both NAD+ and NADP+. Also acts on deamino coenzymes [cf. EC 1.6.1.2 NAD(P)+ transhydrogenase (Re/Si-specific)].
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CAS REGISTRY NUMBER
COMMENTARY
9014-18-0
not distinguished from EC 1.6.1.2
9072-60-0
not distinguished from EC 1.6.1.2
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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
NAD(P)H + 2,6-dichlorophenolindophenol
NAD(P)+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
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+
-
diaphorase-type reactions with NAD(P)H, K3Fe(CN)6 and 2,6-dichlorophenol indophenol
-
?
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+
-
degree of reversibility depends on source of enzyme
-
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 + 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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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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
reduction of FAD leads to its dissociation at enzyme concentrations of 10-100 nM and 30°C-40°C, the apoenzyme can be reactivated to 10-15% by addition of FAD
FAD
-
FAD dissociates from the enzyme by heat treatment at 100°C or by treatment with 5% trichloroacetic acid at 0°C
FAD
-
inactivation by heat treatment can be reversed by addition of FAD
FAD
-
inactivation by heat treatment can be reversed by addition of FAD
FAD
-
inactivation by heat treatment can be reversed by addition of FAD
FAD
-
inactivation by heat treatment can be reversed by addition of FAD
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Mn2+
-
compared to Ca2+ 10 times higher concetrations are required to obtain the same degree of activation
additional information
Ca2+
-
10-20fold activation of NAD+ reduction by NADPH at alkaline pH in cell-free extracts
Ca2+
-
Ca2+-dependent allosteric conformational change, competitive inhibition of activation by Mg2+
Mg2+
-
10-20fold activation of NAD+ reduction by NADPH at alkaline pH in cell-free extracts
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
ATP
-
5 mM, 81% inhibition of NADP+ reduction, complete inhibition of NAD+ reduction
NADPH
EcSTH activity is strongly inhibited by excess NADPH, but not by thio-NAD+; the enzyme is strongly inhibited by excess NADPH
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
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
-
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
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
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-hydroxymercuribenzoate
-
activation, depending on presence of oxidized or reduced substrates
2'-AMP
-
activation of reduction of NADP+ or thio-NAD+ by NADH, no effect on reduction of NAD+ or thio-NAD+ by NADPH
2'-AMP
-
partially replaceable by 0.3 mM 2',3'-cyclic AMP or coenzyme A
2'-AMP
-
activation of NADP+ reduction by NADH is strongly Ca2+ dependent at nonsaturating concentrations of 2'-AMP
2'-AMP
-
0.5 mM, 26% activation of NAD+ reduction by NADPH, 12.5% activation of NADP+ reduction by NADPH, 1100% activation of NAD+ reduction by NADH, 21% activation of NADP+ reduction by NADH
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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.
Adrenocortical Carcinoma
Nicotinamide Nucleotide Transhydrogenase as a Novel Treatment Target in Adrenocortical Carcinoma.
Atherosclerosis
Absence of Nicotinamide Nucleotide Transhydrogenase in C57BL/6J Mice Exacerbates Experimental Atherosclerosis.
Bacteremia
Acinetobacter baumannii Genes Required for Bacterial Survival during Bloodstream Infection.
Breast Neoplasms
Transcription Levels of nicotinamide nucleotide transhydrogenase and Its Antisense in Breast Cancer Samples.
Carcinoma, Hepatocellular
Nicotinamide nucleotide transhydrogenase acts as a new prognosis biomarker in hepatocellular carcinoma.
Carcinoma, Hepatocellular
Pyridine-adenine dinucleotide transhydrogenase activity in cells cultured from rat hepatoma.
Carcinoma, Non-Small-Cell Lung
LncRNA NNT-AS1 promotes lung squamous cell carcinoma progression by regulating the miR-22/FOXM1 axis.
Carcinoma, Non-Small-Cell Lung
Nicotinamide nucleotide transhydrogenase regulates mitochondrial metabolism in NSCLC through maintenance of Fe-S protein function.
Cardiomyopathies
Mylk3 null C57BL/6N mice develop cardiomyopathy, whereas Nnt null C57BL/6J mice do not.
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?
Hypertension
Nicotinamide nucleotide transhydrogenase activity impacts mitochondrial redox balance and the development of hypertension in mice.
Infections
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.
Lung Neoplasms
LncRNA NNT-AS1 promotes lung squamous cell carcinoma progression by regulating the miR-22/FOXM1 axis.
Lung Neoplasms
LncRNA NNT-AS1 regulates the progression of lung cancer through the NNT-AS1/miR-3666/E2F2 axis.
Lung Neoplasms
Nicotinamide nucleotide transhydrogenase regulates mitochondrial metabolism in NSCLC through maintenance of Fe-S protein function.
Malaria
NAD(P) transhydrogenase has vital non-mitochondrial functions in malaria parasite transmission.
Metabolic Diseases
A Direct Comparison of Metabolic Responses to High Fat Diet in C57BL/6J and C57BL/6NJ Mice.
Multiple Sclerosis
Nicotinamide nucleotide transhydrogenase expression analysis in multiple sclerosis patients.
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
Long non-coding RNA NNT-AS1 functions as an oncogenic gene through modulating miR-485/BCL9 in cholangiocarcinoma.
Neoplasms
Long noncoding RNA NNT-AS1 enhances the malignant phenotype of bladder cancer by acting as a competing endogenous RNA on microRNA-496 thereby increasing HMGB1 expression.
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
Nicotinamide nucleotide transhydrogenase acts as a new prognosis biomarker in hepatocellular carcinoma.
Neoplasms
Studies on the isocitrate dehydrogenase. II. Isocitrate dehydrogenase and transhydrogenase in tumor bearing rat liver and ascites tumor cells.
Neoplasms
Upregulated expression of LncRNA nicotinamide nucleotide transhydrogenase antisense RNA 1 is correlated with unfavorable clinical outcomes in cancers.
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?
Osteosarcoma
Upregulation of long non-coding RNA NNT-AS1 promotes osteosarcoma progression by inhibiting the tumor suppressive miR-320a.
Stomach Neoplasms
Downregulation of nicotinamide nucleotide transhydrogenase and its naturally occurring antisense RNA in gastric cancer.
Stomach Neoplasms
Nicotinamide nucleotide transhydrogenase-mediated redox homeostasis promotes tumor growth and metastasis in gastric cancer.
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
dependency on Mg2+ concentration
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10.5
-
pH 7.0: about 55% of maximal activity, pH 10.5: about 45% of maximal activity
8.4 - 8.7
-
half maximal activity in this pH range in the absence of Ca2+ or Mg2+, no activity above
9.1 - 9.3
-
half maximal activity in this pH range in the presence of 5 mM Ca2+ or Mg2+, no activity above
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
two pyridine nucleotide transhydrogenases: the energy-independent soluble pyridine nucleotide transhydrogenase (STH or UdhA) (EC 1.6.1.1) and the membrane-bound, energy-dependent pyridine nucleotide transhydrogenase (TH or PntAB) (EC 1.6.1.2). PntAB is widely distributed in the mitochondria and some bacteria, while STH is found only in certain Gammaproteobacteria and gram-positive bacteria
physiological function
the soluble pyridine nucleotide transhydrogenase, STH, is an energy-independent flavoprotein that directly catalyzes hydride transfer between NAD(H) and NADP(H) to maintain homeostasis of these two redox cofactors
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
421000
52000
54000
421000
-
purified enzyme: exceptional stability of polymers at neutral pH
52000
-
x * 52000, model of quarternary structure, SDS-PAGE, immunoblot
54000
-
8 * 54000, four subunits are placed in a rhomb, a second tetramer is located staggered on top of the first one, deduced from amino acid analysis and electron micrography of purified enzyme
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
octamer
octamer
-
8 * 54000, four subunits are placed in a rhomb, a second tetramer is located staggered on top of the first one, deduced from amino acid analysis and electron micrography of purified enzyme
octamer
-
x * 52000, model of quarternary structure, SDS-PAGE, immunoblot
octamer
-
8 * 54000, four subunits are placed in a rhomb, a second tetramer is located staggered on top of the first one, deduced from amino acid analysis and electron micrography of purified enzyme
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
50
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
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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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
urea, 8 M, no dissociation, complete inactivation of enzyme activity in 5 M urea
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM Tris-HCl, pH 7.0, 2 mM dithiothreitol, several weeks, no loss of activity, great loss of activity after several months
-
4°C, 0.1 M phosphate buffer, pH 7.5, 1 mM EDTA, several months, no loss of activity, storage at -20°C yields a partly insoluble enzyme
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Escherichia coli strain is transformed with a two plasmid system, one encoding the udhA gene and the other one encoding the phb operon
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
inactivation by 4 M guanidinium HCl, 4-6% reactivation after transfer in 100 mM Tris buffer, pH 7.5 containing 100 mM FAD
-
urea inactivation: 3% reactivation after dialysis against buffer containing 0.1 mM FAD, 35% after dialysis against buffer containing 1% mercaptoethanol and 95% reactivation after dialysis against buffer containing both 0.1 mM FAD and 1% mercaptoethanol
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
biotechnology
-
enzymatic NADH production system in reverse micelles using a bacterial glycerol dehydrogenase. The present system is further extended to NADPH production in reverse micelles by coupling with a bacterial soluble transhydrogenase that catalyses the conversion of NADP+ to NADPH using NADH. Glycerol dehydrogenase and soluble transhydrogenase have potential for use in redox cofactor recycling in reverse micelles, which allows the use of catalytic quantities of NAD(P)H in organic media
biotechnology
-
Escherichia coli strain is transformed with a two plasmid system, one encoding the udhA gene and the other one encoding the phb operon. The functionality of this particular system is successfully demonstrated in PHB production experiments. Both productivity and yield of PHB can be increased when NADPH availability is increased
biotechnology
-
enzymatic NADH production system in reverse micelles using a bacterial glycerol dehydrogenase. The present system is further extended to NADPH production in reverse micelles by coupling with a bacterial soluble transhydrogenase that catalyses the conversion of NADP+ to NADPH using NADH. Glycerol dehydrogenase and soluble transhydrogenase have potential for use in redox cofactor recycling in reverse micelles, which allows the use of catalytic quantities of NAD(P)H in organic media
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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Pseudomonas fluorescens
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Pisum sativum, Solanum tuberosum
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