1.97.1.4: [formate-C-acetyltransferase]-activating enzyme
This is an abbreviated version!
For detailed information about [formate-C-acetyltransferase]-activating enzyme, go to the full flat file.
Word Map on EC 1.97.1.4
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1.97.1.4
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glycyl
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5\'-deoxyadenosyl
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iron-sulfur
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organometallic
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adomet
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oxygen-sensitive
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homolytic
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endor
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adenosylmethionine
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5'-deoxyadenosine
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h-atom
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sulfonium
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knappe
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deoxyadenosyl
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medicine
- 1.97.1.4
-
glycyl
-
5\'-deoxyadenosyl
-
iron-sulfur
-
organometallic
- adomet
-
oxygen-sensitive
-
homolytic
-
endor
- adenosylmethionine
- 5'-deoxyadenosine
-
h-atom
-
sulfonium
-
knappe
-
deoxyadenosyl
- medicine
Reaction
Synonyms
Activase, pyruvate formate-lyase, Formate acetyltransferase activase, Formate-lyase-activating enzyme, PFL, PFL activase, PFL activating enzyme, PFL-activating enzyme, PFL-AE, PFL-glycine:S-adenosyl-L-methionine H transferase (flavodoxin-oxidizing, S-adenosyl-L-methionine-cleaving), PflA, pyruvate formate lyase activating enzyme, Pyruvate formate-lyase activase, Pyruvate formate-lyase activating enzyme, pyruvate formate-lyase-activating enzyme
ECTree
1.97.1.4 [formate-C-acetyltransferase]-activating enzymeAdvanced search results
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General Information on EC 1.97.1.4 - [formate-C-acetyltransferase]-activating enzyme
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
pyruvate formate-lyase activating enzyme (PFL-AE) is a member of the large and diverse radical S-adenosyl-L-methionine (SAM) superfamily, members of which use an iron-sulfur cluster and SAM to initiate difficult radical transformations in all kingdoms of life. Radical SAM enzymes share a common CX3CX2C motif or variation thereof, and the conserved cysteines coordinate three irons of a [4Fe-4S] cluster, while SAM coordinates the fourth iron through its amino and carboxylate moieties
malfunction
mutation of either pflB, which codes for PFL, or pflA, which codes for pyruvate formate lyase activating enzyme, results in abrogation of mixed acid fermentation on galactose, and leads to a decrease in pneumococcal virulence
metabolism
physiological function
metabolism
enzyme is activated by pyruvate formate-lyase-activating enzyme by generating a catalytically essential radical on residue Gly734. In the open conformation of the enzyme, the Gly734 residue is located not in its buried position in the enzyme active site but rather in a more solvent-exposed location. The presence of the activating enzyme increases the proportion of enzyme in the open conformation. The activating enzyme accesses residue Gly734 for direct hydrogen atom abstraction by binding to the Gly734 loop in the open conformation, thereby shifting the closed open equilibrium of the enzyme to the right
metabolism
multiple regulators control the transcription of pflA and pflB, some of these regulators are induced by galactose, their control over pflA and pflB is influenced by sodium formate, they exert regulatory influence on each other, and are required for pneumococcal colonization and virulence. Transcriptional profile of mutant DELTApflB compared to the wild-type D39 strain, expression of seven genes annotated as transcriptional regulators is either significantly up or downregulated in the mutant, overview. CcpA, GlnR, and GntR interact with the putative promoters of pflA and pflB, impact of formate on binding affinity of CcpA and GlnR
physiological function
pyruvate formate-lyase-activating enzyme (PFL-AE) activates pyruvate formate-lyase
physiological function
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holo-flavodoxin is capable of associating with NADP+-dependent flavodoxin oxidoreductase and pyruvate formate-lyase activating enzyme, whereas there is no detectable interaction between apo-flavodoxin. Holo-flavodoxin interacts with pyruvate formate-lyase activating enzyme with a dissociation constant of 23.3 microM
physiological function
PFL-AE is a radical S-adenosyl-L-methionine enzyme that utilizes an iron-sulfur cluster and S-adenosyl-L-methionine to activate pyruvate formate lyase (PFL) via pro-S hydrogen abstraction from Gly734
physiological function
pyruvate formate lyase (PFL), converting pyruvate to formate and acetyl-CoA, is the key enzyme for mixed acid fermentation. Active pyruvate formate lyase (PFL) synthesis is finely tuned, and feedback inhibition and activation involving the pyruvate formate lyase activating enzyme, are detected, analysis of the transcriptional regulation of gene pflA, overview. The pyruvate formate lyase activating enzyme (PFL-AE) is responsible for posttranslational activation of inactive PFL
physiological function
pyruvate formate-lyase activating enzyme (PFL-AE) is a radical S-adenosyl-L-methionine (SAM) enzyme that installs a catalytically essential glycyl radical on pyruvate formate lyase
physiological function
Escherichia coli B / ATCC 11303
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holo-flavodoxin is capable of associating with NADP+-dependent flavodoxin oxidoreductase and pyruvate formate-lyase activating enzyme, whereas there is no detectable interaction between apo-flavodoxin. Holo-flavodoxin interacts with pyruvate formate-lyase activating enzyme with a dissociation constant of 23.3 microM
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