Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.6.1.2 extracted from

  • Ronchi, J.A.; Francisco, A.; Passos, L.A.; Figueira, T.R.; Castilho, R.F.
    The contribution of nicotinamide nucleotide transhydrogenase to peroxide detoxification is dependent on the respiratory state and counterbalanced by other sources of NADPH in liver mitochondria (2016), J. Biol. Chem., 291, 20173-20187 .
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Mus musculus 5739
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
NADPH + NAD+ Mus musculus
-
NADP+ + NADH
-
?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADPH + 3-acetylpyridine adenine dinucleotide
-
Mus musculus NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
?
NADPH + NAD+
-
Mus musculus NADP+ + NADH
-
?

Synonyms

Synonyms Comment Organism
nicotinamide nucleotide transhydrogenase
-
Mus musculus
NNT
-
Mus musculus

General Information

General Information Comment Organism
malfunction lack of enzyme activity impairs peroxide metabolism in intact mitochondria Mus musculus