Information on EC 1.6.1.2 - NAD(P)+ transhydrogenase (Re/Si-specific)

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.6.1.2
-
RECOMMENDED NAME
GeneOntology No.
NAD(P)+ transhydrogenase (Re/Si-specific)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NADPH + NAD+ = NADP+ + NADH
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
NAD/NADH phosphorylation and dephosphorylation
-
-
NAD metabolism
-
-
Nicotinate and nicotinamide metabolism
-
-
Metabolic pathways
-
-
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 hide
9014-18-0
not distinguished from EC 1.6.1.1
9072-60-0
not distinguished from EC 1.6.1.1
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene Nnt
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
NADH + NADP+
NAD+ + NADPH
show the reaction diagram
NADH + NADP+
NADPH + NAD+
show the reaction diagram
NADH + oxidized 3-acetylpyridine adenine dinucleotide
NAD+ + reduced 3-acetylpyridine adenine dinucleotide
show the reaction diagram
-
-
-
-
?
NADH + thio-NADP+
NAD+ + thio-NADPH
show the reaction diagram
NADP+ + NADH
NADPH + NAD+
show the reaction diagram
NADPH + 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
show the reaction diagram
NADPH + 3-acetylpyridine-NAD(P)+
NADP+ + 3-acetylpyridine-NAD(P)H
show the reaction diagram
-
-
-
-
r
NADPH + 3-acetylpyridine-NAD+
3-acetylpyridine-NADH + NADP+
show the reaction diagram
NADPH + NAD+
NADP+ + NADH
show the reaction diagram
NADPH + NAD+ + H+/in
NADP+ + NADH + H+/out
show the reaction diagram
-
-
-
r
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
show the reaction diagram
-
-
-
-
?
NADPH + oxidized 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
show the reaction diagram
NMNH + thio-NADP+
NMN + thio-NADPH
show the reaction diagram
-
-
-
?
thio-NADH + NADP+
thio-NAD+ + NADPH
show the reaction diagram
-
poor substrate
-
-
r
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
NADH + NADP+
NAD+ + NADPH
show the reaction diagram
NADH + NADP+
NADPH + NAD+
show the reaction diagram
NADP+ + NADH
NADPH + NAD+
show the reaction diagram
NADPH + NAD+
NADP+ + NADH
show the reaction diagram
NADPH + NAD+ + H+/in
NADP+ + NADH + H+/out
show the reaction diagram
Q24858
-
-
-
r
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)+
NAD(P)H
additional information
-
no flavin cofactor, differentiation from EC 1.6.1.1.
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
no activation
Li+
-
not clear whether this reflects a general salt effect or a Li+ specific effect
Na+
-
not clear whether this reflects a general salt effect or a Na+ specific effect
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2',5'-ADP
-
bacteriorhodopsin co-reconstituted enzyme, 36.8% inhibition of thio-NADP+ reduction by NADH in the dark, 34.4% in the light
2'-AMP
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
3'-5'-AMP
-
-
3'-AMP
-
-
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'-AMP
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-CoA
-
-
acetyl-dephospho-CoA
-
competitive vs. NAD(H)
acetylpyridine adenine dinucleotide
-
-
adenosine
ADP
-
-
Butane-2,3-dione
-
-
cardiolipin
-
noncompetitive vs. NAD+ and NADPH
D2O
-
-
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
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
N-ethylmaleimide
Na+
-
200 mM, 50% inhibition at pH 7.9, 300 mM, 40% inhibition at pH 5.5, 95% at pH 8.5
NADP+
NADPH
p-chloromercuribenzoate
p-Chlororomercuriphenyl sulfonate
-
-
palmitoyl CoA
-
specifically interferes with Nnt activity by competition with NADPH-binding, 20% residual activity at 1 mM
palmitoyl-CoA
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
Phenylarsine oxide
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
triiodothyronine
additional information
-
NNT expression is 2.8fold downregulated in the vastus lateralis muscle of calorie restricted rhesus monkeys
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
asolectin
-
10fold stimulation of partially purified enzyme
-
Carbonyl cyanide m-chlorophenylhydrazone
cardiolipin
-
10fold stimulation of partially purified enzyme with Escherichia coli cardiolipin
ecdysone
-
-
H2O2
-
136% increase of activity at 0.5 mM
lecithin
-
5fold stimulation of partially purified enzyme
Lipids
-
-
-
lysolecithin
-
aprrox. 0.3%, 150% activation of activity in chromatophore extracts
phosphatidylcholine
-
-
Phospholipids
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.028 - 0.166
acetylpyridine adenine dinucleotide
0.028 - 0.125
NAD+
0.003 - 0.063
NADH
0.0017 - 0.04
NADP+
0.014 - 0.03
NADPH
2.6 - 3.4
NMNH
0.06 - 0.8
oxidized acetylpyridine adenine dinucleotide
-
0.012 - 0.063
thio-NADP+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02 - 1.44
oxidized acetylpyridine adenine dinucleotide
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7 - 8
2'-AMP
0.003
2,4-Dinitrophenyl-3'-dephospho-CoA
-
-
0.4
3'-5'-AMP
-
-
0.7
3'-AMP
-
-
0.3 - 3.7
5'-AMP
0.2
acetyl-CoA
-
-
0.011
acetyl-dephospho-CoA
-
-
0.007
acetylpyridine adenine dinucleotide
-
-
0.5
adenosine
-
-
0.3
ADP
-
-
0.2
CoA
0.009
dephospho-CoA
-
-
2.5
Mg2+
-
at pH 7.0
0.17
NADP+
-
vs. NADPH
0.0035 - 0.26
NADPH
0.00015 - 0.01
palmitoyl-CoA
0.093 - 0.12
reduced acetylpyridine adenine dinucleotide
0.0003
S-7-nitrobenzofuran-4-yl-3'-dephospho-CoA
-
-
0.0026
S-7-Nitrobenzofuran-4-yl-CoA
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.044
-
activity in membranes of strain AB1450
0.19
-
reduction of acetylpyridine adenine dinucleotide by NADPH
0.26
-
activity in inside-out membrane vesicles at pH 7.4, presence of an uncoupler i.e. carbonylcyanide-m-chlorophylhydrazone results in 2fold stimulation
2.6
-
partially purified enzyme
12 - 15
-
-
13.6
-
partially purified enzyme, assay in the presence of Escherichia coli phospholipids
16.2
-
-
24.6
-
reduction of 3-acetylpyridine adenine dinucleotide
35.6
-
reduction of 3-acetylpyridine adenine dinucleotide
50.8
-
native enzyme with acetylpyridine-NAD+ a n NADPH as substrates, pH 7.0
62.3
-
-
additional information
-
no activity detected with the insertion mutants
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 6.5
-
rapid decline above, cyclic reaction
6.2 - 6.3
-
-
6.5
-
assay at
7 - 8
-
reduction of oxidized acetylpyridine adenine dinucleotide by NADPH in inside-out membrane vesicles
7
-
reduction of NAD+
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.7 - 6.7
-
less than 50% of maximal activity above and below
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
high expression level
Manually annotated by BRENDA team
-
very strong expression
Manually annotated by BRENDA team
-
bone marrow-derived, Nnt mRNA and protein are expressed in resting macrophages and down-regulated in response to inflammatory stimuli such as lipopolysaccharide. Nnt mRNA and protein expression are further repressed in fully activated macrophages; bone marrow-derived, Nnt mRNA and protein are expressed in resting macrophages and down-regulated in response to inflammatory stimuli such as lipopolysaccharide. Nnt mRNA and protein expression are repressed in fully activated macrophages
Manually annotated by BRENDA team
-
high expression level
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Sinorhizobium meliloti (strain SM11)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6784
-
x * 6784, soluble component, amino acid analysis
28000
-
dIII fragement, SDS-PAGE
40000
-
dI fragement, SDS-PAGE
47000
-
alpha2,beta2, 2 * 50000 + 2 * 47000
48667
-
alpha2,beta2, 2 * 53906 + 2 * 48667, calculation from nucleotide sequence
50000
-
alpha2,beta2, 2 * 50000 + 2 * 47000
53906
-
alpha2,beta2, 2 * 53906 + 2 * 48667, calculation from nucleotide sequence
54000
-
x * 54000, immunoblot with antibodies against beef heart enzyme
66000
-
2 * 66000, SDS-PAGE
97000
-
x * 97000, SDS-PAGE
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
109212
-
2 * 109212, calculated from cDNA sequence
110000
111500
-
2 * 111500, SDS-PAGE
115000
-
2 * 115000, SDS-PAGE
120000
155000
196000
-
-
206000 - 249000
-
cross-linking of purified enzyme with 10.9 mM dimethyl suberimidate dihydrochloride
210000 - 230000
250000
-
-
278000
-
radiation inactivation, hydrodynamic properties
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
-
monomer
-
solution of isolated dIII domains
tetramer
trimer
-
trimers of dI2dIII1 are formes in mixed solutions containing dI and dIII domains
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospholipoprotein
-
5 mol loosely bound phospholipids, 9 mol tightly bound phospholipids
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dIII domain
-
dIII domain
-
dIII domain in its thio-NADP+ form
-
dI2dIII complex in its thio-NAD+/NADP+ form
-
dI2dIII1 complex and dI domain
-
dIII domain, vapor diffusion method
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 6
-
activity decreases as the pH approaches 6.0, although a second minor peak is evident at pH 5.0, the activity of the nonenergy-linked reaction decreases with medium acidification and activity loss is most notable at pH 4.0
695903
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
5 min, soluble component, complete inactivation
44
-
2 min, solubilized membrane component, 50% inactivation
45
-
incubation of depleted membranes, inactivation of membrane transhydrogenase component
48
-
2 min, membrane particles, 50% inactivation
50
-
complete protection in the presence of NADPH, half-maximal protection with 0.01 mM NADPH
53
-
incubation for 3 min, 10 mM Mg2+ almost completely protect from inactivation
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
cations prevent from tryptic inactivation, 95% protection with Mn2+, 89% with Ca2+ and 79% with Mg2+
-
inactivation during prolonged column chromatography
-
solubilized membrane component is unstable loosing all activity when stored overnight at 4C or -70C, stable at -70C in the presence of 0.025 mM NADP+ for several months, inactivation by refreezing after thawing
-
trypsinolysis is stimulated several fold by NADPH and NADP+, half-maximal stimulation with 0.001-0.002 mM NADPH and 0.002-0.003 mM NADP+, Mg2+ protects from NADP+ stimulated inactivation
-
unstable, loses 30-50% activity within 48 h at 4C, remainder of the enzyme becomes inactive after 2 weeks, complete inactivation after freezing at -20C or -70C overnight, enzyme is very susceptible to trypsinolysis, NADH protects from tryptic inactivation, NADPH promotes tryptic inactivation
-
urea, 6 M, inactivation
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,1-dimethylbutanol
-
inactivation
Acetone
-
used for conversion of mitochondria to an acetone powder causes inactivation
Ethanol
-
10%, 40C, inactivation
n-Butanol
-
inactivation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C or 4C, Rhodospirillum rubrum membrane component, inactivation in 1 day, stabilization by NADP+
-
-80C, 25% glycerol
-
4C, 0.1 M sodium phosphate buffer, pH 7.5, 1 mM dithiothreitol, 0.05% sodium cholate
-
4C, reconstituted with phospholipids, stable for at least 2 months
-
4C, unsoluble component: 0.1 M glycyl-glycine buffer, pH 8.0, 10% sucrose, unstable, soluble factor: 120 h with 0.015 mM dithiothreitol stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatography
affinity chromatography on NADP+/NAD+-agarose gels, partial purification
-
affinity chromatography; NaCl wash, Triton X-100 extraction, affinity chromatography on immobilized NAD+
-
FPLC in the presence of 0.05 or 0.1% Triton X-100, comparison of methods
-
fractionation of submitochondrial particles, DEAE-Sepharose, hydroxyapatite
-
immunoexclusion chromatography
-
Ni-NTA column chromatography
Nnt is purified using an immunocapture bead matrix
-
overview of early procedures
-
partially purified
-
recombinant domain I
-
recombinant domain III
-
recombinant domain III-domain I protein
-
recombinant domains I and III
-
recombinant enzyme
-
recombinant protein
-
recombinant protein using His-tag
recombinant proteins
-
soluble component
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
as Corynebacterium glutamicum does not possess membrane-integral nicotinamide nucleotide transhydrogenase, the Escherichia coli pntAB genes are expressed in the genetically defined Corynebacterium glutamicum lysine-producing strain DM1730, resulting in membrane-associated transhydrogenase activity of 0.7 U/mg proteine. Expression of the pntAB genes in Corynebacterium glutamicum improves L-lysine formation. In contrast, pntAB expression has a negative effect on growth and glutamate production of Corynebacterium glutamicum wild type
-
dI and native and E155W mutant of dIII expressed in Escherichia coli
-
dIII domain expressed in Escherichia coli
-
domains dIII and dI expressed in Escherichia coli, recombiant protein lacks the membrane spanning dII domain
-
expressed in Corynebacterium glutamicum strain ATCC 13032
expressed in Escherichia coli as His-tag fusion protein
expressed in Escherichia coli B834 (DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
-
expression in Escherichia coli on multicopy plasmid
-
expression of domain I in Escherichia coli
-
expression of domain I Y235N and Y235F mutants in Escherichia coli
-
expression of domain III-domain I protein in Escherichia coli
-
expression of domains I and III in Escherichia coli
-
expresssion of domain III in Escherichia coli
-
gene Nnt, overexpression of C-terminally V5-tagged full-length cDNA in the macrophage-like cell line RAW264.7, real-time PCR expression analysis
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Nnt activity is reduced by 18% in the heart failure
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reconstitution into liposomes
Show AA Sequence (14231 entries)
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