PROSITE documentation PDOC51554Pyruvate 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.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Leppaenen V.-M. Merckel M.C. Ollis D.L. Wong K.K. Kozarich J.W. Goldman A. |
| Title | Pyruvate formate lyase is structurally homologous to type I ribonucleotide reductase. | |
| Source | Structure 7:733-744(1999). | |
| PubMed ID | 10425676 |
| 2 | Authors | Lehtioe L. Grossmann J.G. Kokona B. Fairman R. Goldman A. |
| Title | Crystal structure of a glycyl radical enzyme from Archaeoglobus fulgidus. | |
| Source | J. Mol. Biol. 357:221-235(2006). | |
| PubMed ID | 16414072 | |
| DOI | 10.1016/j.jmb.2005.12.049 |
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