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Information on EC 1.6.1.2 - NAD(P)+ transhydrogenase (Re/Si-specific) and Organism(s) Homo sapiens

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EC Tree
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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This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
pntab, energy-linked transhydrogenase, mitochondrial transhydrogenase, proton-translocating transhydrogenase, proton-translocating nicotinamide nucleotide transhydrogenase, nadph transhydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dII
-
-
-
-
dIII
-
-
-
-
energy-linked transhydrogenase
-
-
-
-
H+-thase
-
-
-
-
NAD transhydrogenase
-
-
-
-
NAD(P) transhydrogenase
-
-
-
-
NADH transhydrogenase
-
-
-
-
NADH-NADP-transhydrogenase
-
-
-
-
NADPH transhydrogenase
-
NADPH-NAD oxidoreductase
-
-
-
-
NADPH-NAD transhydrogenase
-
-
-
-
NADPH:NAD+ transhydrogenase
-
-
-
-
nicotinamide adenine dinucleotide (phosphate) transhydrogenase
-
-
-
-
nicotinamide nucleotide transhydrogenase
proton-translocating nicotinamide nucleotide transhydrogenase
-
-
proton-translocating transhydrogenase
-
pyridine nucleotide transferase
-
-
-
-
pyridine nucleotide transhydrogenase
-
-
-
-
transhydrogenase
-
-
-
-
transhydrogenase, nicotinamide adenine dinucleotide (phosphate)
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
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
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
NADPH + 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
show the reaction diagram
-
-
-
?
NADPH + NAD+
NADP+ + NADH
show the reaction diagram
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
show the reaction diagram
NATURAL SUBSTRATE
NATURAL 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
NADPH + NAD+
NADP+ + NADH
show the reaction diagram
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)+
NAD(P)H
NAD+
-
-
NADH
-
-
NADP+
-
-
NADPH
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
34% residual activity at 1 mM
palmitoyl CoA
specifically interferes with Nnt activity by competition with NADPH-binding, 20% residual activity at 1 mM
S-nitrosoglutathione
100% inhibition at 3 mM or higher concentration
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
H2O2
136% increase of activity at 0.5 mM
additional information
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
enzyme knockdown decreases reductive carboxylation and stimulates glucose catabolism in the tricarboxylic acid cycle
metabolism
physiological function
the enzyme plays a role in reactive oxygen species detoxification in human adrenal glands
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NNTM_HUMAN
1086
12
113896
Swiss-Prot
Secretory Pathway (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
two monomers with dI, dII, and dIII domain structure
homodimer
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
dIII domain
-
dIII domain in its thio-NADP+ form
PROTEIN VARIANTS
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
F215S
G200S
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
S193N
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Nnt is purified using an immunocapture bead matrix
recombinant domain III
-
recombinant protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
dIII domain expressed in Escherichia coli
expressed in Escherichia coli B834 (DE3) cells
expresssion of domain III in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Nnt activity is reduced by 18% in the heart failure
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Peake, S.J.; Venning, J.D.; Jackson, J.B.
A catalytically active complex formed from the recombinant dI protein of Rhodospirillum rubrum transhydrogenase, and the recombinant dIII protein of the human enzyme
Biochim. Biophys. Acta
1411
159-169
1999
Homo sapiens, Rhodospirillum rubrum
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Arkblad, E.L.; Egorov, M.; Shakhparonov, M.; Romanova, L.; Polzikov, M.; Rydstrom, J.
Expression of proton-pumping nicotinamide nucleotide transhydrogenase in mouse, human brain and C. elegans
Comp. Biochem. Physiol. B
133
13-21
2002
Caenorhabditis elegans, Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Singh, A.; Venning, J.D.; Quirk, P.G.; van Boxel, G.I.; Rodrigues, D.J.; White, S.A.; Jackson, J.B.
Interactions between transhydrogenase and thio-nicotinamide Analogues of NAD(H) and NADP(H) underline the importance of nucleotide conformational changes in coupling to proton translocation
J. Biol. Chem.
278
33208-33216
2003
Rhodospirillum rubrum, Homo sapiens (Q13423)
Manually annotated by BRENDA team
Sheeran, F.L.; Rydstroem, J.; Shakhparonov, M.I.; Pestov, N.B.; Pepe, S.
Diminished NADPH transhydrogenase activity and mitochondrial redox regulation in human failing myocardium
Biochim. Biophys. Acta
1797
1138-1148
2010
Homo sapiens (Q13423), Homo sapiens
Manually annotated by BRENDA team
Meimaridou, E.; Kowalczyk, J.; Guasti, L.; Hughes, C.; Wagner, F.; Frommolt, P.; Nuernberg, P.; Mann, P.; Banerjee, R.; Saka, H.N.; Chapple, J.P.; King, P.J,; Clark, A.J.L.; Metherell, L.A.
Mutations in NNT encoding nicotinamide nucleotide transhydrogenase cause familial glucocorticoid deficiency
Nat. Genet.
44
740-742
2012
Homo sapiens (Q13423)
Manually annotated by BRENDA team
White, S.A.; Peake, S.J.; McSweeney, S.; Leonard, G.; Cotton, N.P.; Jackson, J.B.
The high-resolution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from human heart mitochondria
Structure
8
1-12
2000
Homo sapiens (Q13423), Homo sapiens
Manually annotated by BRENDA team
Fujisawa, Y.; Napoli, E.; Wong, S.; Song, G.; Yamaguchi, R.; Matsui, T.; Nagasaki, K.; Ogata, T.; Giulivi, C.
Impact of a novel homozygous mutation in nicotinamide nucleotide transhydrogenase on mitochondrial DNA integrity in a case of familial glucocorticoid deficiency
BBA Clin.
3
70-78
2015
Homo sapiens (Q13423)
Manually annotated by BRENDA team
Scott, R.; Van Vliet, G.; Deladoey, J.
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
Eur. J. Endocrinol.
176
C1-C2
2017
Homo sapiens
Manually annotated by BRENDA team
Metherell, L.A.; Guerra-Assuncao, J.A.; Sternberg, M.J.; David, A.
three-dimensional model of human nicotinamide nucleotide transhydrogenase (NNT) and sequence-structure analysis of its disease-causing variations
Hum. Mutat.
37
1074-1084
2016
Homo sapiens (Q13423)
Manually annotated by BRENDA team
Gameiro, P.A.; Laviolette, L.A.; Kelleher, J.K.; Iliopoulos, O.; Stephanopoulos, G.
Cofactor balance by nicotinamide nucleotide transhydrogenase (NNT) coordinates reductive carboxylation and glucose catabolism in the tricarboxylic acid (TCA) cycle
J. Biol. Chem.
288
12967-12977
2013
Homo sapiens
Manually annotated by BRENDA team
Weinberg-Shukron, A.; Abu-Libdeh, A.; Zhadeh, F.; Carmel, L.; Kogot-Levin, A.; Kamal, L.; Kanaan, M.; Zeligson, S.; Renbaum, P.; Levy-Lahad, E.; Zangen, D.
Combined mineralocorticoid and glucocorticoid deficiency is caused by a novel founder nicotinamide nucleotide transhydrogenase mutation that alters mitochondrial morphology and increases oxidative stress
J. Med. Genet.
52
636-641
2015
Homo sapiens
Manually annotated by BRENDA team