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Literature summary for 1.2.1.10 extracted from

  • Kessler, D.; Leibrecht, I.; Knappe, J.
    Pyruvate-formate-lyase-deactivase and acetyl-CoA reductase activities of Escherichia coli reside on a polymeric protein particle encoded by adhE (1991), FEBS Lett., 281, 59-63.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene adhE, pyruvate-formate-lyase-deactivase with alcohol and acetaldehyde dehydrogenase activity Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ 3fold activation with 0.00003 mM, 5fold activation with 0.03 mM, activation only of NADH oxidation, not NAD+ reduction Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
96000
-
ca. 40 * 96000, pyruvate-formate-lyase-deactivase with alcohol and aldehyde dehydrogenase activity, nucleotide sequence Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetaldehyde + CoA + NAD+ Escherichia coli
-
acetyl-CoA + NADH
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
grown anaerobically
-

Purification (Commentary)

Purification (Comment) Organism
from anaerobically grown cells, rod-shaped Escherichia coli

Storage Stability

Storage Stability Organism
-60°C, 20 mM MOPS-KOH pH 7.6, 0.1 mM EDTA, up to one year Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetaldehyde + CoA + NAD+
-
Escherichia coli acetyl-CoA + NADH
-
?
acetaldehyde + CoA + NAD+
-
Escherichia coli acetyl-CoA + NADH
-
r
acetyl-CoA + NADH
-
Escherichia coli acetaldehyde + CoA + NAD+
-
r

Subunits

Subunits Comment Organism
polymer ca. 40 * 96000, pyruvate-formate-lyase-deactivase with alcohol and aldehyde dehydrogenase activity, nucleotide sequence Escherichia coli

Cofactor

Cofactor Comment Organism Structure
CoA
-
Escherichia coli
NAD+
-
Escherichia coli