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Literature summary for 1.6.1.3 extracted from

  • Bergkvist, A.; Johansson, C.; Johansson, T.; Rydström, J.; Karlsson, g.
    Interactions of the NADP(H)-binding domain III of proton-translocating transhydrogenase from Escherichia coli with NADP(H) and the NAD(H)-binding domain I studied by NMR and site-directed mutagenesis (2000), Biochemistry, 39, 12595-12605.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Escherichia coli

Protein Variants

Protein Variants Comment Organism
A432C the mutant shows altered NADP(H) binding and domain interaction properties Escherichia coli
G430C the mutant shows altered NADP(H) binding and domain interaction properties Escherichia coli
R425C the mutant shows almost exclusively changes in the NADP(H)-binding properties, without changing the affinity for transhydrogenase domain I from Rhodospirillum rubrum Escherichia coli
T393C the mutant shows altered NADP(H) binding and domain interaction properties Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
NADPH + NAD+ Escherichia coli
-
NADP+ + NADH
-
r

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADPH + NAD+
-
Escherichia coli NADP+ + NADH
-
r

Synonyms

Synonyms Comment Organism
proton-translocating transhydrogenase domain III
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Escherichia coli