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Literature summary for 2.3.1.54 extracted from

  • Crain, A.; Broderick, J.
    Pyruvate formate-lyase and its activation by pyruvate formate-lyase activating enzyme (2014), J. Biol. Chem., 289, 5723-5729 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.54

Activating Compound

Activating Compound Comment Organism Structure
pyruvate formate-lyase activating enzyme PFL-AE, EC 1.97.1.4, is a radical S-adenosyl-L-methionine enzyme that utilizes an iron-sulfur cluster and S-adenosyl-L-methionine to activate pyruvate formate lyase (PFL) via pro-S hydrogen abstraction from Gly734. Usage of an S-adenosyl-L-methionine binding assay to accurately determine the equilibrium constants for S-adenosyl-L-methionine binding to enzyme PFL-AE alone and in complex with substrate PFL, activation of PFL in the presence of its substrate pyruvate or the analogue oxamate results in stoichiometric conversion of the [4Fe-4S]1+ cluster to the glycyl radical on PFL. 3.7fold less activation is achieved in the absence of these small molecules, demonstrating that pyruvate or oxamate are required for optimal activation. For the assay, the enzyme PFL-AE is attached to a CM5 sensor chip using standard thiol coupling procedures. PFL activation studies, binding kinetics, overview Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics and equilibrium constant for the enzyme's interaction with activating enzyme PFL-AE, the interaction is very slow and rate-limited by large conformational changes, circular dichroism study 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
-
 r

Organism

Organism UniProt Comment Textmining
Escherichia coli P09373
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CoA + pyruvate
-
 Escherichia coli acetyl-CoA + formate
-
 r

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
 Escherichia coli
[4Fe-4S]-center the [4Fe-4S] cluster of enzyme PFL-AE is coordinated by the cysteines of a conserved CX3CX2C motif, with the fourth unique iron coordinated by S-adenosyl-L-methionine. PFL-AE contains six cysteine residues (Cys12, Cys29, Cys33, Cys36, Cys94, Cys102) and only Cys29, Cys33, and Cys36 are involved in coordinating the iron sulfur cluster Escherichia coli

General Information

General Information Comment Organism
physiological function pyruvate formate-lyase (PFL) supplies the citric acid cycle with acetyl-CoA during anaerobic glycolysis by catalyzing the formation of acetyl-CoA and formate from CoA and pyruvate, and is a central enzyme in anaerobic metabolism of Escherichia coli and other facultative anaerobes. PFL is a glycyl radical enzyme, which play key roles in anaerobic metabolism in microbes, including the reduction of ribonucleotides to deoxyribonucleotides, synthesis of benzylsuccinate, and conversion of choline to trimethylamine Escherichia coli