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Information on EC 7.1.1.1 - proton-translocating NAD(P)+ transhydrogenase and Organism(s) Homo sapiens and UniProt Accession Q13423

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IUBMB Comments
The enzyme is a membrane bound proton-translocating pyridine nucleotide transhydrogenase that couples the reversible reduction of NADP by NADH to an inward proton translocation across the membrane. In the bacterium Escherichia coli the enzyme provides a major source of cytosolic NADPH. Detoxification of reactive oxygen species in mitochondria by glutathione peroxidases depends on NADPH produced by this enzyme.
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Homo sapiens
UNIPROT: Q13423
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
proton-pumping nicotinamide nucleotide transhydrogenase, proton-translocating nad(p)+ transhydrogenase, proton translocating nicotinamide nucleotide transhydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NNT
-
-
-
-
pntA
-
-
-
-
pntB
-
-
-
-
proton-translocating transhydrogenase
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
NADPH:NAD+ oxidoreductase (H+-transporting)
The enzyme is a membrane bound proton-translocating pyridine nucleotide transhydrogenase that couples the reversible reduction of NADP by NADH to an inward proton translocation across the membrane. In the bacterium Escherichia coli the enzyme provides a major source of cytosolic NADPH. Detoxification of reactive oxygen species in mitochondria by glutathione peroxidases depends on NADPH produced by this enzyme.
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 + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
show the reaction diagram
-
-
-
-
r
NADPH + oxidized acetyl pyridine adenine dinucleotide + H+[side 1]
NADP+ + reduced acetyl pyridine adenine dinucleotide + H+[side 2]
show the reaction diagram
-
-
-
-
r
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
links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, provides NADPH for biosynthesis and glutathione reduction
-
-
r
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
show the reaction diagram
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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
Mitochondrion (Reliability: 5)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
monomer composed of three domains dI, dII, and dIII
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
dIII domain in the presence of NADPH
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
dIII domain expressed in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
peripheral blood mononuclear cells from obese (BMI >30) compared to lean subjects have lower NNT and glutathione expression
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mather, O.C.; Singh, A.; van Boxel, G.I.; White, S.A.; Jackson, J.B.
Active-site conformational changes associated with hydride transfer in proton-translocating transhydrogenase
Biochemistry
43
10952-10964
2004
Rhodospirillum rubrum, Rhodospirillum rubrum (Q2RSB2), Homo sapiens (Q13423)
Manually annotated by BRENDA team
Jackson, J.B.; Peake, S.J.; White, S.A.
Structure and mechanism of proton-translocating transhydrogenase
FEBS Lett.
464
1-8
1999
Escherichia coli, Homo sapiens, Rhodospirillum rubrum
Manually annotated by BRENDA team
McCambridge, G.; Agrawal, M.; Keady, A.; Kern, P.; Hasturk, H.; Nikolajczyk, B.; Bharath, L.
Saturated fatty acid activates T cell inflammation through a nicotinamide nucleotide transhydrogenase (Nnt)-dependent mechanism
Biomolecules
9
79
2019
Homo sapiens (Q13423)
Manually annotated by BRENDA team
Chortis, V.; Taylor, A.E.; Doig, C.L.; Walsh, M.D.; Meimaridou, E.; Jenkinson, C.; Rodriguez-Blanco, G.; Ronchi, C.L.; Jafri, A.; Metherell, L.A.; Hebenstreit, D.; Dunn, W.B.; Arlt, W.; Foster, P.A.
Nicotinamide nucleotide transhydrogenase as a novel treatment target in adrenocortical carcinoma
Endocrinology
159
2836-2849
2018
Homo sapiens (Q13423)
Manually annotated by BRENDA team
Favia, M.; Atlante, A.
Cellular redox state acts as switch to determine the direction of NNT-catalyzed reaction in cystic fibrosis cells
Int. J. Mol. Sci.
22
967
2021
Homo sapiens (Q13423)
Manually annotated by BRENDA team
Ward, N.P.; Kang, Y.P.; Falzone, A.; Boyle, T.A.; DeNicola, G.M.
Nicotinamide nucleotide transhydrogenase regulates mitochondrial metabolism in NSCLC through maintenance of Fe-S protein function
J. Exp. Med.
217
e20191689
2020
Homo sapiens (Q13423), Mus musculus (Q61941)
Manually annotated by BRENDA team
Rao, K.; Shen, X.; Pardue, S.; Krzywanski, D.
Nicotinamide nucleotide transhydrogenase (NNT) regulates mitochondrial ROS and endothelial dysfunction in response to angiotensin II
Redox Biol.
36
101650
2020
Homo sapiens (Q13423)
Manually annotated by BRENDA team