PROSITE documentation PDOC51554
Pyruvate formate lyase (PFL) domain profile


Pyruvate formate lyase (PFL) catalyzes the non-oxidative conversion of pyruvate and CoA to formate and acetyl-CoA. Several other enzymes have been identified in the pyruvate formate lyase family: ketoacid formate lyase, glycerol dehydratase (GD), benzyl succinate synthetase and p-hydroxyphenylacetate decarboxylase [1,2].

The PFL domain has a unique α/β barrel arrangement, with five 'up' strands and three 'down' strands; the up and down strands are linked by a unique β finger that carries a key thiyl radical (see <PDB:1QHM>) [1,2].

The profile we developed covers the entire PFL domain.

Last update:

December 2011 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

PFL, PS51554; Pyruvate formate-lyase domain profile  (MATRIX)


1AuthorsLeppaenen V.-M. Merckel M.C. Ollis D.L. Wong K.K. Kozarich J.W. Goldman A.
TitlePyruvate formate lyase is structurally homologous to type I ribonucleotide reductase.
SourceStructure 7:733-744(1999).
PubMed ID10425676

2AuthorsLehtioe L. Grossmann J.G. Kokona B. Fairman R. Goldman A.
TitleCrystal structure of a glycyl radical enzyme from Archaeoglobus fulgidus.
SourceJ. Mol. Biol. 357:221-235(2006).
PubMed ID16414072

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