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Literature summary for 1.6.1.2 extracted from

  • Bizouarn, T.; Fjellstrom, O.; Meuller, J.; Axelsson, M.; Bergkvist, A.; Johansson, C.; Goran Karlsson, B.; Rydstrom, J.
    Proton translocating nicotinamide nucleotide transhydrogenase from E. coli. Mechanism of action deduced from its structural and catalytic properties (2000), Biochim. Biophys. Acta, 1457, 211-228.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Escherichia coli
-
-
-
Rhodospirillum rubrum
-
-
-

Reaction

Reaction Comment Organism Reaction ID
NADPH + NAD+ = NADP+ + NADH hypothetical mechanism Escherichia coli
NADPH + NAD+ = NADP+ + NADH hypothetical mechanism Bos taurus
NADPH + NAD+ = NADP+ + NADH hypothetical mechanism Rhodospirillum rubrum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADPH + oxidized 3-acetylpyridine adenine dinucleotide enzyme also catalyzes a rapid, so called cyclic reaction, i.e. the reduction of acetylpyridine adenine dinucleotide in the presence of either NADP+ or NADPH: the NADPH/NADP+ remain permanently bound to domain III and are alternately oxidized by acetylpyridine adenine dinucleotide and then reduced by NADH in domain I Escherichia coli NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
?
NADPH + oxidized 3-acetylpyridine adenine dinucleotide enzyme also catalyzes a rapid, so called cyclic reaction, i.e. the reduction of acetylpyridine adenine dinucleotide in the presence of either NADP+ or NADPH: the NADPH/NADP+ remain permanently bound to domain III and are alternately oxidized by acetylpyridine adenine dinucleotide and then reduced by NADH in domain I Bos taurus NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
?
NADPH + oxidized 3-acetylpyridine adenine dinucleotide enzyme also catalyzes a rapid, so called cyclic reaction, i.e. the reduction of acetylpyridine adenine dinucleotide in the presence of either NADP+ or NADPH: the NADPH/NADP+ remain permanently bound to domain III and are alternately oxidized by acetylpyridine adenine dinucleotide and then reduced by NADH in domain I Rhodospirillum rubrum NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
?

Subunits

Subunits Comment Organism
dimer
-
Bos taurus
tetramer
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Escherichia coli
NAD+
-
Bos taurus
NAD+
-
Rhodospirillum rubrum
NADH
-
Escherichia coli
NADH
-
Bos taurus
NADH
-
Rhodospirillum rubrum
NADP+
-
Escherichia coli
NADP+
-
Bos taurus
NADP+
-
Rhodospirillum rubrum
NADPH
-
Escherichia coli
NADPH
-
Bos taurus
NADPH
-
Rhodospirillum rubrum