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Literature summary for 7.1.1.1 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
Search for more literature for 7.1.1.1

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
D135N mutation has no effect in binding affinity of either NAD+ or NADH Rhodospirillum rubrum
D135N the mutant shows reduced activity compared to the wild type enzyme Rhodospirillum rubrum
E155W the mutant shows reduced activity compared to the wild type enzyme Rhodospirillum rubrum
Q132N the mutant shows reduced activity compared to the wild type enzyme Rhodospirillum rubrum
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
R127A the mutant shows reduced activity compared to the wild type enzyme Rhodospirillum rubrum
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
R127M the mutant shows reduced activity compared to the wild type enzyme Rhodospirillum rubrum
S135A mutation has no effect in binding affinity of either NAD+ or NADH Rhodospirillum rubrum
S138A the mutant shows reduced activity compared to the wild type enzyme Rhodospirillum rubrum

Localization

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
NADPH + NAD+ + H+[side 1] Rhodospirillum rubrum
-
 NADP+ + NADH + H+[side 2]
-
 ?

Organism

Organism UniProt Comment Textmining
Rhodospirillum rubrum
-
-
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
transhydrogenase
-
 Rhodospirillum rubrum