IPR012838
Pyruvate formate-lyase 1 activating enzyme
InterPro entry
Short name | PFL1_activating |
Overlapping homologous superfamilies | |
family relationships |
Description
Pyruvate formate lyase-activating enzyme
1.97.1.4 is a 28kDa monomeric protein which is involved in the anerobic glucose metabolism pathway. It is a member of the radical S-adenosylmethionine family of enzymes which initiate radical catalysis. It is necessary to activate pyruvate formate lyase (PFL), which catalyses the conversion of pyruvate and coenzyme A to formate and acetyl CoA.
Pyruvate formate lyase activating enzyme functions by catalysing the formation of the Gly734 radical of PFL. It utilises a [4Fe-4S] cluster and adenosylmethionine to generate a putative adenosyl radical, which extracts a hydrogen atom from Gly734 on PFL, thus activating PFL for catalysis
[1]. Members of this family are iron-sulphur proteins with a radical-SAM domain.
References
1.Pyruvate formate-lyase activating enzyme: elucidation of a novel mechanism for glycyl radical formation. Buis JM, Broderick JB. Arch. Biochem. Biophys. 433, 288-96, (2005). View articlePMID: 15581584
GO terms
biological process
- None
molecular function
cellular component
- None
Cross References
ENZYME
Genome Properties
Contributing Member Database Entry
- NCBIfam:TIGR02493