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Literature summary for 1.18.1.1 extracted from

  • Marczak, R.; Ballongue, J.; Petitdemange, H.; Gay, R.
    Regulation of the biosynthesis of NADH-rubredoxin oxidoreductase in Clostridium acetobutylicum (1984), Curr. Microbiol., 10, 165-168.
No PubMed abstract available

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
NADH + oxidized rubredoxin Clostridium acetobutylicum the induction of rubredoxin reductase, normally observed at pH 4.3 is stopped immediately after the addition of rifampicin. The enzyme could play a role in some deacidification mechanism in relation to proton transport NAD+ + reduced rubredoxin
-
?

Organism

Organism UniProt Comment Textmining
Clostridium acetobutylicum
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADH + oxidized rubredoxin
-
Clostridium acetobutylicum NAD+ + reduced rubredoxin
-
?
NADH + oxidized rubredoxin the induction of rubredoxin reductase, normally observed at pH 4.3 is stopped immediately after the addition of rifampicin. The enzyme could play a role in some deacidification mechanism in relation to proton transport Clostridium acetobutylicum NAD+ + reduced rubredoxin
-
?

Cofactor

Cofactor Comment Organism Structure
FAD prosthetic group Clostridium acetobutylicum
NADH
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Clostridium acetobutylicum