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Literature summary extracted from

  • Lehtioe, L.; Grossmann, J.G.; Kokona, B.; Fairman, R.; Goldman, A.
    Crystal structure of a glycyl radical enzyme from Archaeoglobus fulgidus (2006), J. Mol. Biol., 357, 221-235.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.54 purified enzyme, sitting drop vapour diffusion method, mixing 0.001 ml of 20 mg/ml protein solution with 0.001 ml precipitant solution containing 16% w/v PEG 8000, 8% v/v isopropanol, 80 mM Hepes, pH 7.5, 160 mM ammonium sulfate and 1 mM DTT, plate-like crystals, X-ray diffraction structure determination and analysis at 2.9 A resolution Archaeoglobus fulgidus

General Stability

EC Number General Stability Organism
2.3.1.54 PFL2 appears to be stabilized by several factors including an increased number of ion pairs, differences in buried charges, a truncated N terminus, anchoring of loops and N terminus via salt-bridges,changes in the oligomeric interface and perhaps also the higher oligomerization state of the protein Archaeoglobus fulgidus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.54 95000
-
 4 * 95000, structure analysis, crystal packing, solution X-ray scattering, and ultracentrifugation Archaeoglobus fulgidus
2.3.1.54 297000
-
 dynamic light scattering, analytical ultracentrifugation Archaeoglobus fulgidus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.54 CoA + pyruvate Archaeoglobus fulgidus
-
 acetyl-CoA + formate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.54 Archaeoglobus fulgidus
-
 a hyperthermophile, gene pfl2
-
4.2.1.30 Clostridium butyricum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.54 native enzyme at pH 6.4, by anion exchange and hydrophobic interaction chromatography, and gel filtration, to homogeneity Archaeoglobus fulgidus

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.54 acetyl-CoA + formate = CoA + pyruvate active site structure includes an active site tunnel, substrate binding at Asp447 at the protein surface Archaeoglobus fulgidus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.54 CoA + pyruvate
-
 Archaeoglobus fulgidus acetyl-CoA + formate
-
 ?
2.3.1.54 additional information the enzyme is a glycyl radical enzyme, changes in the active site indicate that the actual substrate of PFL2 is bigger than a glycerol molecule, but sequence and structural homology suggest that PFL2 may be a dehydratase Archaeoglobus fulgidus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.54 tetramer 4 * 95000, structure analysis, crystal packing, solution X-ray scattering, and ultracentrifugation Archaeoglobus fulgidus

Synonyms

EC Number Synonyms Comment Organism
2.3.1.54 PFL
-
 Archaeoglobus fulgidus
2.3.1.54 pyruvate formate lyase
-
 Archaeoglobus fulgidus
4.2.1.30 glycerol dehydratase
-
 Clostridium butyricum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.54 7.5
-
 assay at Archaeoglobus fulgidus