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Literature summary extracted from

  • Brondijk, T.H.; van Boxel, G.I.; Mather, O.C.; Quirk, P.G.; White, S.A.; Jackson, J.B.
    The role of invariant amino acid residues at the hydride transfer site of proton-translocating transhydrogenase (2006), J. Biol. Chem., 281, 13345-13354.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
7.1.1.1 mutant enzymes are crystallized by the hanging drop vapor diffusion method, using in 16-24% (w/v) 8K-PEG, 20-150 mM (NH4)2SO4, 100mM MES, pH 6.0, and 10% (v/v) glycerol in the presence of 50 mM NAD+ and 5 mM NADP+ Rhodospirillum rubrum

Protein Variants

EC Number Protein Variants Comment Organism
7.1.1.1 D135N mutation has no effect in binding affinity of either NAD+ or NADH Rhodospirillum rubrum
7.1.1.1 D135N the mutant shows reduced activity compared to the wild type enzyme Rhodospirillum rubrum
7.1.1.1 E155W the mutant shows reduced activity compared to the wild type enzyme Rhodospirillum rubrum
7.1.1.1 Q132N the mutant shows reduced activity compared to the wild type enzyme Rhodospirillum rubrum
7.1.1.1 R127A mutation strongly inhibits the rate of transhydrogenation and alters the nucleotide-binding properties of the dI protein. When dIR127A is reconstituted into the intact enzyme in membranes, transhydrogenation rates are negligible. dI is the NAD(H)-binding component of the transhydrogenase Rhodospirillum rubrum
7.1.1.1 R127A the mutant shows reduced activity compared to the wild type enzyme Rhodospirillum rubrum
7.1.1.1 R127M mutation strongly inhibits the rate of transhydrogenation and alters the nucleotide-binding properties of the dI protein. When dIR127M is reconstituted into the intact enzyme in membranes, transhydrogenation rates are negligible. dI is the NAD(H)-binding component of the transhydrogenase Rhodospirillum rubrum
7.1.1.1 R127M the mutant shows reduced activity compared to the wild type enzyme Rhodospirillum rubrum
7.1.1.1 S135A mutation has no effect in binding affinity of either NAD+ or NADH Rhodospirillum rubrum
7.1.1.1 S138A the mutant shows reduced activity compared to the wild type enzyme Rhodospirillum rubrum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.1.1.1 membrane
-
 Rhodospirillum rubrum 16020
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
7.1.1.1 40000
-
 2 * 40000, SDS-PAGE Rhodospirillum rubrum

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] Rhodospirillum rubrum
-
 NADP+ + NADH + H+[side 2]
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.1 Rhodospirillum rubrum
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.1.1 NADPH + NAD+ + H+[side 1]
-
 Rhodospirillum rubrum NADP+ + NADH + H+[side 2]
-
 ?
7.1.1.1 NADPH + oxidized acetyl pyridine adenine dinucleotide + H+[side 1]
-
 Rhodospirillum rubrum NADP+ + reduced acetyl pyridine adenine dinucleotide + H+[side 2]
-
 r

Subunits

EC Number Subunits Comment Organism
7.1.1.1 homodimer 2 * 40000, SDS-PAGE Rhodospirillum rubrum

Synonyms

EC Number Synonyms Comment Organism
7.1.1.1 transhydrogenase
-
 Rhodospirillum rubrum