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Literature summary extracted from

  • Fjellström, O.; Axelsson, M.; Bizouarn, T.; Hu, X.; Johansson, C.; Meuller, J.; Rydström, J.
    Mapping of residues in the NADP(H)-binding site of proton-translocating nicotinamide nucleotide transhydrogenase from Escherichia coli (1999), J. Biol. Chem., 274, 6350-6359.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.1.1.1
-
 Rhodospirillum rubrum
7.1.1.1 expression of cysteine mutants A348C, A390C, K424C, and R425C in Escherichia coli Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
7.1.1.1 A348C mutation introduced into a cysteine-free mutant enzyme, mutant shows markedly reduced activity Escherichia coli
7.1.1.1 A390C mutation introduced into a cysteine-free mutant enzyme Escherichia coli
7.1.1.1 K424C mutation introduced into a cysteine-free mutant enzyme, mutant shows markedly reduced activity Escherichia coli
7.1.1.1 R425C mutation introduced into a cysteine-free mutant enzyme, mutant shows markedly reduced activity Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.1.1.1 2-(4-maleimidoanilino)-naphthalene-6-sulfonic acid 0.004 mM, 2 h incubation, 75% inhibition of reverse reaction catalyzed by A348C mutant enzyme, 95% inhibition of A390C mutant enzyme after 1 h, 90% inhibition of K424C mutant enzyme after 1 h, 55% inhibition of R425C mutant enzyme after 1h Escherichia coli
7.1.1.1 3-Aminopyridine adenine dinucleotide phosphate competitive vs. NADP(H) Escherichia coli
7.1.1.1 N-ethylmaleimide 0.2 mM, 57% inhibition of reverse reaction in A348C mutant enzyme, 60% inhibition of K424C mutant enzyme, more than 95% inhibition of A390C mutant enzyme after 1h, R425C mutant enzyme is not inhibited Escherichia coli
7.1.1.1 N-ethylmaleimide
-
 Rhodospirillum rubrum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.1.1.1 0.014
-
 NADPH cysteine-free mutant enzyme Escherichia coli
7.1.1.1 0.023
-
 NADPH A348C mutation introduced into cysteine-free mutant enzyme Escherichia coli
7.1.1.1 0.033
-
 NADPH A390C mutation introduced into cysteine-free mutant enzyme Escherichia coli
7.1.1.1 0.04
-
 NADPH K424C mutation introduced into cysteine-free mutant enzyme Escherichia coli
7.1.1.1 0.12
-
 NADPH R425C mutation introduced into cysteine-free mutant enzyme Escherichia coli

Organism

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

Subunits

EC Number Subunits Comment Organism
7.1.1.1 tetramer domain I, i.e. alpha1 to alpha404, and III i.e. beta260 to beta462, are exposed to the cytosol and contain the binding sites for NAD(H) and NAD(P)H, respectively, domain II, i.e. alpha405 to alpha 510, spans the membrane Escherichia coli

Cofactor

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

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
7.1.1.1 0.1
-
 3-Aminopyridine adenine dinucleotide phosphate approximate value Escherichia coli