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Information on EC 1.6.1.2 - NAD(P)+ transhydrogenase (Re/Si-specific) and Organism(s) Escherichia coli and UniProt Accession P07001
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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: Escherichia coli
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
enzyme is stereospecific for the 4A hydrogen of NADH and the 4B hydrogen of NADPH
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
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
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 + 3-acetylpyridine-NAD+
3-acetylpyridine-NADH + NADP+
-
-
-
-
?
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
-
?
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
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
-
?
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
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
-
NADH
-
-
NADP+
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
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
adenosine
-
bacteriorhodopsin co-reconstituted enzyme, 54.2% inhibition of thio-NADP+ reduction by NADH in the dark, 16.0% in the light
glutathione
-
protection by NADP+ or NAD+, presence of NADPH accelerates inhibition
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
NAD+
-
bacteriorhodopsin co-reconstituted enzyme, 61.5% inhibition of thio-NADP+ reduction by NADH in the dark, 18.4% in the light
reduced acetylpyridine adenine dinucleotide
-
competitive vs. oxidized acetylpyridine dinucleotide, noncompetitive 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
-
bacteriorhodopsin co-reconstituted enzyme, 54.6% inhibition of thio-NADP+ reduction by NADH in the dark, 24.3% in the light
5'-AMP
-
competitive vs acetylpyridine adenine dinucleotide, noncompetitive vs. NADPH
NADPH
-
bacteriorhodopsin co-reconstituted enzyme, 76.9% inhibition of thio-NADP+ reduction by NADH in the dark, 57.4% in the light
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cardiolipin
-
10fold stimulation of partially purified enzyme with Escherichia coli cardiolipin
Phospholipids
-
approx. 15fold stimulation of partially purified enzyme with crude Escherichia coli lipid fraction
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.063
NADH
-
enzyme co-reconstituted with bacteriorhodopsin, in the presence of the uncoupler carbonyl cyanide m-chloro-phenylhydrazone
0.012
thio-NADP+
-
enzyme co-reconstituted with bacteriorhodopsin, in the dark
0.013
thio-NADP+
-
enzyme co-reconstituted with bacteriorhodopsin, in the light
0.063
thio-NADP+
-
enzyme co-reconstituted with bacteriorhodopsin, in the presence of the uncoupler carbonyl cyanide m-chloro-phenylhydrazone
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.12
reduced acetylpyridine adenine dinucleotide
-
vs. oxidized acetylpyridine adenine dinucleotide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
13.6
-
partially purified enzyme, assay in the presence of Escherichia coli phospholipids
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
-
reduction of oxidized acetylpyridine adenine dinucleotide by NADH i.e. forward reaction
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
48667
-
alpha2,beta2, 2 * 53906 + 2 * 48667, calculation from nucleotide sequence
53906
-
alpha2,beta2, 2 * 53906 + 2 * 48667, calculation from nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
monomer is split into PntA and PntB chain, enzyme displays an overall dimeric structure
tetramer
tetramer
-
alpha2,beta2, 2 * 53906 + 2 * 48667, calculation from nucleotide sequence
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hoek, J.B.; Rydström, J.; Höjeberg, B.
Comparative studies on nicotinamide nucleotide transhydrogenase from different sources
Biochim. Biophys. Acta
333
237-245
1974
Escherichia coli
Jackson, J.B.; Lever, T.M.; Rydström, J.; Persson, B.; Carlenor, E.
Proton-translocating transhydrogenase from photosynthetic bacteria
Biochem. Soc. Trans.
19
573-575
1991
Escherichia coli, Mammalia
Clarke, D.M.; Loo, T.W.; Gillam, S.; Bragg, P.D.
Nucleotide sequence of the pntA and pntB genes encoding the pyridine nucleotide transhydrogenase of Escherichia coli
Eur. J. Biochem.
158
647-653
1986
Escherichia coli
Clarke, D.M.; Bragg, P.D.
Expression of the cloned subunits of Escherichia coli transhydrogenase from separate replicons
FEBS Lett.
200
23-26
1986
Escherichia coli
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
Hanson, R.L.
The kinetic mechanism of pyridine nucleotide transhydrogenase from Escherichia coli
J. Biol. Chem.
254
888-893
1979
Escherichia coli
Rydström, J.
Energy-linked nicotinamide nucleotide transhydrogenases
Biochim. Biophys. Acta
463
155-184
1977
Bos taurus, Escherichia coli, Rattus norvegicus, Rhodospirillum rubrum
Houghton, R.L.; Fisher, R.R.; Sanadi, D.R.
Dependence of Escherichia coli pyridine nucleotide transhydrogenase on phospholipids and its sensitivity
Biochem. Biophys. Res. Commun.
73
751-757
1976
Escherichia coli
Fristedt, U.; Rydström, J.; Persson, B.
Evidence for a nicotineamide nucleotide transhydrogenase in Klebsiella pneumoniae
Biochem. Biophys. Res. Commun.
198
928-932
1994
Escherichia coli, Klebsiella pneumoniae
Hu, X.; Zhang, J.W.; Persson, A.; Rydstrom, J.
Characterization of the interaction of NADH with proton pumping E. coli transhydrogenase reconstituted in the absence and in the presence of bacteriorhodopsin
Biochim. Biophys. Acta
1229
64-72
1995
Escherichia coli
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
Kabus, A.; Georgi, T.; Wendisch, V.F.; Bott, M.
Expression of the Escherichia coli pntAB genes encoding a membrane-bound transhydrogenase in Corynebacterium glutamicum improves L-lysine formation
Appl. Microbiol. Biotechnol.
75
47-53
2007
Escherichia coli
Yamauchi, Y.; Hirasawa, T.; Nishii, M.; Furusawa, C.; Shimizu, H.
Enhanced acetic acid and succinic acid production under microaerobic conditions by Corynebacterium glutamicum harboring Escherichia coli transhydrogenase gene pntAB
J. Gen. Appl. Microbiol.
60
112-118
2014
Escherichia coli (P07001), Escherichia coli
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