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Literature summary for 1.97.1.4 extracted from

  • Conradt, H.; Hohmann-Berger, M.; Hohmann, H.P.; Blaschkowski, H.P.; Knappe, J.
    Pyruvate formate-lyase (inactive form) and pyruvate formate-lyase activating enzyme of Escherichia coli: isolation and structural properties (1984), Arch. Biochem. Biophys., 228, 133-142.
    View publication on PubMed
Search for more literature for 1.97.1.4

Activating Compound

Activating Compound Comment Organism Structure
additional information contains a covalently bound chromophoric factor which has an optical absorptiion peak at 388 nm Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
29500
-
 1 * 29500, SDS-PAGE Escherichia coli
34000
-
 gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.017
-
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine formate acetyltransferase-glycine is the inactive form of the enzyme Escherichia coli 5'-deoxyadenosine + methionine + flavodoxin + formate acetyltransferase-glycine-2-yl-radical formate acetyltransferase-glycine-2-yl-radical is the active form of the enzyme ?

Subunits

Subunits Comment Organism
monomer 1 * 29500, SDS-PAGE Escherichia coli