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Literature summary for 7.1.1.2 extracted from

  • Elguindy, M.M.; Nakamaru-Ogiso, E.
    Apoptosis-inducing factor (AIF) and its family member protein, AMID, are rotenone-sensitive NADH ubiquinone oxidoreductases (NDH-2) (2015), J. Biol. Chem., 290, 20815-20826 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
2-n-heptyl-4-hydroxyquinoline-N-oxide
-
Homo sapiens
rotenone
-
Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Homo sapiens 16020
-
mitochondrion
-
Homo sapiens 5739
-

Organism

Organism UniProt Comment Textmining
Homo sapiens O95831
-
-
Homo sapiens Q9BRQ8
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.77
-
pH 7.0, 30°C, N-terminally tagged protein Homo sapiens
7.52
-
pH 7.0, 30°C, N-terminally tagged protein Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADH + oxidized coenzyme Q1 + 5 H+[side1]
-
Homo sapiens NAD+ + reduced coenzyme Q1 + 4 H+[side2]
-
?

Synonyms

Synonyms Comment Organism
AIF-homologous mitochondrion-associated inducer of death
-
Homo sapiens
AIFM1
-
Homo sapiens
AIFM2
-
Homo sapiens
AmiD
-
Homo sapiens
apoptosis-inducing factor 1
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FAD
-
Homo sapiens
additional information no cofactor: deamino-NADH Homo sapiens
NADH
-
Homo sapiens

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00075
-
2-n-heptyl-4-hydroxyquinoline-N-oxide pH 7.0, 30°C, N-terminally tagged protein Homo sapiens
0.00104
-
2-n-heptyl-4-hydroxyquinoline-N-oxide pH 7.0, 30°C, N-terminally tagged protein Homo sapiens

General Information

General Information Comment Organism
physiological function after reconstituting isolated AIFM1 into bacterial or mitochondrial membranes, N-terminally tagged AIFM1 displays substantial NADH:O2 activity and supports NADH-linked proton pumping activities in the host membranes. Overexpressing N-terminally tagged AIFM1 and AIF-homologous mitochondrion-associated inducer of death AMID enhances the growth of a double knock-out Escherichia coli strain lacking complex I and NDH-2. C-terminally tagged AIFM1 and NADH-binding site mutants of N-terminally tagged AIFM1 and AMID fail to show both NADH:O2 activity and the growth-enhancing effect Homo sapiens
physiological function after reconstituting isolated AIFM2 into bacterial or mitochondrial membranes, N-terminally tagged AIFM2 displays substantial NADH:O2 activity and supports NADH-linked proton pumping activities in the host membranes. Overexpressing N-terminally tagged AIFM1 and AIFM2 enhances the growth of a double knock-out Escherichia coli strain lacking complex I and NDH-2. NADH-binding site mutants of N-terminally tagged AIFM1 and AIFM2 fail to show both NADH:O2 activity and the growth-enhancing effect Homo sapiens