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Literature summary for 7.1.1.1 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
Search for more literature for 7.1.1.1

Cloned(Commentary)

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

Protein Variants

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

Inhibitors

Inhibitors Comment Organism Structure
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
3-Aminopyridine adenine dinucleotide phosphate competitive vs. NADP(H) Escherichia coli
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
N-ethylmaleimide
-
 Rhodospirillum rubrum

KM Value [mM]

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

Organism

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

Subunits

Subunits Comment Organism
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

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

Ki Value [mM]

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