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Literature summary for 7.1.1.1 extracted from

  • Johansson, C.; Pedersen, A.; Karlsson, B.G.; Rydstroem, J.
    Redox-sensitive loops D and E regulate NADP(H) binding in domain III and domain I-domain III interactions in proton-translocating Escherichia coli transhydrogenase (2002), Eur. J. Biochem., 269, 4505-4515.
    View publication on PubMed
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Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
A398C the mutant with wild type activity shows increased ratios between the rates of the forward and reverse reactions, thus approaching that of the wild type enzyme Escherichia coli
A432C the mutant shows increased ratios between the rates of the forward and reverse reactions, thus approaching that of the wild type enzyme Escherichia coli
D392C the mutant shows increased ratios between the rates of the forward and reverse reactions, thus approaching that of the wild type enzyme Escherichia coli
G408C the mutant with wild type activity shows increased ratios between the rates of the forward and reverse reactions, thus approaching that of the wild type enzyme Escherichia coli
G430C the mutant shows increased ratios between the rates of the forward and reverse reactions, thus approaching that of the wild type enzyme Escherichia coli
I406C the mutant with 450% of wild type activity shows increased ratios between the rates of the forward and reverse reactions, thus approaching that of the wild type enzyme Escherichia coli
M409C the mutant with 75% of wild type activity shows increased ratios between the rates of the forward and reverse reactions, thus approaching that of the wild type enzyme Escherichia coli
S404C the mutant with 75% of wild type activity shows increased ratios between the rates of the forward and reverse reactions, thus approaching that of the wild type enzyme Escherichia coli
T393C the mutant shows increased ratios between the rates of the forward and reverse reactions, thus approaching that of the wild type enzyme Escherichia coli
V411C the mutant with 125% of wild type activity shows increased ratios between the rates of the forward and reverse reactions, thus approaching that of the wild type enzyme Escherichia coli
Y431C the mutant with 450% of wild type activity shows increased ratios between the rates of the forward and reverse reactions, thus approaching that of the wild type enzyme Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Q-Sepharose column chromatography, and butyl Toyopearl column chromatography Escherichia coli

Substrates and Products (Substrate)

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