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Literature summary 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

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.1.1.1 membrane
-
Escherichia coli 16020
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
7.1.1.1 48000
-
2 * 54000 + 2 * 48000, SDS-PAGE Escherichia coli
7.1.1.1 54000
-
2 * 54000 + 2 * 48000, SDS-PAGE Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.1.1.1 NADPH + NAD+ + H+[side 1] Escherichia coli
-
NADP+ + NADH + H+[side 2]
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.6.1.2 Bos taurus
-
-
-
1.6.1.2 Escherichia coli
-
-
-
1.6.1.2 Rhodospirillum rubrum
-
-
-
7.1.1.1 Escherichia coli
-
-
-

Reaction

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.1.2 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
-
?
1.6.1.2 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
-
?
1.6.1.2 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
-
?
7.1.1.1 NADPH + NAD+ + H+[side 1]
-
Escherichia coli NADP+ + NADH + H+[side 2]
-
?
7.1.1.1 NADPH + oxidized 3-acetylpyridine adenine dinucleotide + H+[side 1]
-
Escherichia coli NADP+ + reduced 3-acetylpyridine adenine dinucleotide + H+[side 2]
-
r
7.1.1.1 thio-NADP+ + NADH + H+[side 2]
-
Escherichia coli thio-NADPH + NAD+ + H+[side 1]
-
r

Subunits

EC Number Subunits Comment Organism
1.6.1.2 dimer
-
Bos taurus
1.6.1.2 tetramer
-
Escherichia coli
7.1.1.1 heterotetramer 2 * 54000 + 2 * 48000, SDS-PAGE Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
7.1.1.1 proton translocating nicotinamide nucleotide transhydrogenase
-
Escherichia coli

Cofactor

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