Literature summary for 2.3.1.54 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.

Search for more literature for 2.3.1.54

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

General Stability	Organism
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]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Archaeoglobus fulgidus	-	a hyperthermophile, gene pfl2	-

Purification (Commentary)

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

Reaction

Reaction	Comment	Organism	Reaction ID
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)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
CoA + pyruvate	-	Archaeoglobus fulgidus	acetyl-CoA + formate	-	?
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

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

Synonyms

Synonyms	Comment	Organism
PFL	-	Archaeoglobus fulgidus
pyruvate formate lyase	-	Archaeoglobus fulgidus

pH Optimum

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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)