NNT dimer transfers proton from NADPH to NAD+

Stable Identifier
R-HSA-450971
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Synonyms
H(+)(in) + NAD(+) + NADPH = H(+)(out) + NADH + NADP(+)
ReviewStatus
5/5
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NNT (nicotinamide nucleotide transhydrogenase) associated with the inner mitochondrial membrane catalyzes the reaction of mitochondrial NADPH and NAD+ to form NADP+ and NADH. The reaction is coupled to the translocation of a proton across the inner mitochondrial membrane into the mitochondrial matrix (Arkblad et al., 1996; White et al., 2000). The active form of NNT is inferred to be a homodimer based on the known structure of its bovine homolog (Yamaguchi & Hatefi, 1991) and the structure of the ovine homolog (Kampjut & Sazanow, 2019). Mutations in NNT can lead to glucocorticoid deficiency (GCCD4; MIM:614736; reviewed in Francisco et al., 2021).
Literature References
PubMed ID Title Journal Year
8616157 The cDNA sequence of proton-pumping nicotinamide nucleotide transhydrogenase from man and mouse

Arkblad, EL, Rydström, J, Betsholtz, C

Biochim Biophys Acta 1996
2005110 Mitochondrial energy-linked nicotinamide nucleotide transhydrogenase. Membrane topography of the bovine enzyme

Yamaguchi, M, Hatefi, Y

J Biol Chem 1991
34155914 Mitochondrial NAD(P)+ Transhydrogenase: From Molecular Features to Physiology and Disease

Figueira, TR, Francisco, A, Castilho, RF

Antioxid Redox Signal 2022
10673423 The high-resolution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from human heart mitochondria

Peake, SJ, Jackson, JB, Leonard, G, McSweeney, S, White, SA, Cotton, NP

Structure 2000
31462775 Structure and mechanism of mitochondrial proton-translocating transhydrogenase

Sazanov, LA, Kampjut, D

Nature 2019
Participants
Participates
Catalyst Activity

NAD(P)+ transhydrogenase activity of NNT dimer [mitochondrial inner membrane]

Orthologous Events
Cross References
RHEA
Rhea
Authored
Reviewed
Created
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