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Literature summary for 2.3.1.54 extracted from

  • Condic-Jurkic, K.; Perchyonok, V.T.; Zipse, H.; Smith, D.M.
    On the modeling of arginine-bound carboxylates: A case study with Pyruvate Formate-Lyase (2008), J. Comput. Chem., 29, 2425-2433.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of the pyruvate formate-lyase monomer in complex with pyruvate and CoA, structure of active site, small model computational studies of the pyruvate formate-lyase substrate transformation Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli P09373
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
mechanistic effect of choosing different protonation states for a substrate carboxylate group that is involved in a salt bridge with an arginine residue analyzed, modeling of arginine-bound carboxylates, computational details, neutral model and anionic model presented, extended model consists of pyruvate in a complex with methylguanidinum and methylthiyl radical, neutral carboxylic acid as a more realistic approximation to the salt bridge arrangement than a bare anionic carboxylate substituent Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CoA + pyruvate
-
Escherichia coli acetyl-CoA + formate
-
?
CoA + pyruvate mechanism to truncate an arginine-bound carboxylate motif, substrate mechanism of pyruvate formate-lyase used as a case study Escherichia coli acetyl-CoA + formate
-
?

Synonyms

Synonyms Comment Organism
PFL
-
Escherichia coli
pyruvate formate-lyase
-
Escherichia coli