Cofactors

There are no Cofactors for this Enzyme

Reaction Mechanism

formate C-acetyltransferase By Reference

Pyruvate formate-lyase catlayses the CoA-dependent, reversible cleavage of pyruvate into acetyal-CoA and formation. This enzyme is required for anaerobic glucose fermentation, utilised by various species of microorganism.

The resting state of this enzyme has a glycyl radical, this radical is created by the action of a radical SAM superfamily activating protein (PFL-AE) and is quenched in an oxygenated atmosphere leading to enzyme inactivation.




• Summary
• Step 1
• Step 2
• Step 3
• Step 4
• Step 5
• Step 6
• Step 7
• Products

The resting state of the enzyme involves the glycyl radical, as determined by spectroscopic studies. The backbone radical is kinetically stable, but extremely susceptible to reactions with molecular oxygen. This is thought to be involved in regulating the enzymes function within the anaerobic metabolism, and the regulation of the pathway more generally.

Catalytic Residues

AA	Uniprot	Uniprot Resid	PDB	PDB Resid
Cys	P09373	419	2pfl	418
Cys	P09373	420	2pfl	419
Trp	P09373	334	2pfl	333
Gly	P09373	735	2pfl	734

Step Components

hydrogen relay, overall reactant used, overall product formed, enzyme-substrate complex formation, bimolecular homolytic substitution, bimolecular homolytic addition, hydrogen transfer, intermediate formation, unimolecular homolytic elimination, intermediate terminated, native state of enzyme regenerated, intermediate collapse, radical propagation, enzyme-substrate complex cleavage



Step 1.

The glycyl radical abstracts a hydrogen from Cys419, which in turn abstracts a hydrogen from Cys418.



Step 2.

Cys418 initiates a homolytic attack on the carbonyl carbon of the pyruvate substrate in an addition reaction.



Step 3.

The newly formed radical collapses, eliminating a carbon dioxyl radical.



Step 4.

The carbon dioxyl radical abstracts a hydrogen from Cys419 forming the formate product.



Step 5.

Cys419 abstracts a hydrogen from CoA.



Step 6.

CoA initiates a homolytic attack upon the carbonyl carbon of the acyl-Cys418 in a substitution reaction, eliminating Cys418, which abstracts a hydrogen from Cys419.



Step 7.

Cys419 abstracts a hydrogen from Gly734, regenerating the glycyl radical ground state.



Products.

The products of the reaction.

View Reaction Mechanisms in M-CSA

Reaction Parameters

There are no kinetic parameters information for this Enzyme

Associated Proteins

Citations

• Oral magnesium prevents acetaminophen-induced acute liver injury by modulating microbial metabolism.
• Phylogenetically and metabolically diverse autotrophs in the world's deepest blue hole.
• De novo assembly and comparative genome analysis for polyhydroxyalkanoates-producing Bacillus sp. BNPI-92 strain.
• The oxygen-tolerant reductive glycine pathway assimilates methanol, formate and CO₂ in the yeast Komagataella phaffii.
• Extracellular vesicles of Pseudomonas aeruginosa downregulate pyruvate fermentation enzymes and inhibit the initial growth of Staphylococcus aureus.
• Transcriptional control of carbohydrate catabolism by the CcpA protein in the ruminal bacterium Streptococcus bovis.
• Rumen Lachnospiraceae isolate NK3A20 exhibits metabolic flexibility in response to substrate and coculture with a methanogen.
• Hydrogenotrophic methanogenesis is the key process in the obligately syntrophic consortium of the anaerobic ameba Pelomyxa schiedti.
• A new metabolic trait in an acetogen: Mixed acid fermentation of fructose in a methylene-tetrahydrofolate reductase mutant of Acetobacterium woodii.
• Metabolomics of Escherichia coli for Disclosing Novel Metabolic Engineering Strategies for Enhancing Hydrogen and Ethanol Production.
• An integrated systems biology approach reveals differences in formate metabolism in the genus Methanothermobacter.