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
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glycyl
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5\'-deoxyadenosyl
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iron-sulfur
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organometallic
- adomet
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oxygen-sensitive
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homolytic
-
endor
- adenosylmethionine
- 5'-deoxyadenosine
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h-atom
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sulfonium
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knappe
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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
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Substrates Products
Substrates Products on EC 1.97.1.4 - [formate-C-acetyltransferase]-activating enzyme
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REACTION DIAGRAM
S-adenosyl-L-methionine + 5-deazariboflavin + [formate C-acetyltransferase]-glycine
5'-deoxyadenosine + L-methionine + 5-deazariboflavin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical
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S-adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine
5'-deoxyadenosine + methionine + flavodoxin + formate acetyltransferase-glycine-2-yl-radical
S-Adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine
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S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine
5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical
S-adenosyl-L-methionine + dihydroflavodoxin + [pyruvate formate-lyase]-glycine
methionine + 5'-deoxyadenosine + [pyruvate formate-lyase]-glycine radical + flavodoxin
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r
S-adenosyl-L-methionine + NADH + formate acetyltransferase-glycine
5'-deoxyadenosine + methionine + NAD+ + formate acetyltransferase-glycine-2-yl-radical
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40% of activity with reduced methyl viologen
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S-adenosyl-L-methionine + NADPH + formate acetyltransferase-glycine
5'-deoxyadenosine + methionine + NADP+ + formate acetyltransferase-glycine-2-yl-radical
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95% of activity with reduced methyl viologen
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S-adenosyl-L-methionine + reduced methyl viologen + formate acetyltransferase-glycine
5'-deoxyadenosine + methionine + methyl viologen + formate acetyltransferase-glycine-2-yl-radical
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5'-deoxyadenosine + methionine + flavodoxin + formate acetyltransferase-glycine-2-yl-radical
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S-adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine
5'-deoxyadenosine + methionine + flavodoxin + formate acetyltransferase-glycine-2-yl-radical
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S-adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine
5'-deoxyadenosine + methionine + flavodoxin + formate acetyltransferase-glycine-2-yl-radical
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S-adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine
5'-deoxyadenosine + methionine + flavodoxin + formate acetyltransferase-glycine-2-yl-radical
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S-adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine
5'-deoxyadenosine + methionine + flavodoxin + formate acetyltransferase-glycine-2-yl-radical
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S-adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine
5'-deoxyadenosine + methionine + flavodoxin + formate acetyltransferase-glycine-2-yl-radical
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?
S-adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine
5'-deoxyadenosine + methionine + flavodoxin + formate acetyltransferase-glycine-2-yl-radical
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?
S-adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine
5'-deoxyadenosine + methionine + flavodoxin + formate acetyltransferase-glycine-2-yl-radical
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?
S-adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine
5'-deoxyadenosine + methionine + flavodoxin + formate acetyltransferase-glycine-2-yl-radical
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?
S-adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine
5'-deoxyadenosine + methionine + flavodoxin + formate acetyltransferase-glycine-2-yl-radical
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?
S-adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine
5'-deoxyadenosine + methionine + flavodoxin + formate acetyltransferase-glycine-2-yl-radical
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formate acetyltransferase-glycine is the inactive form of the enzyme
formate acetyltransferase-glycine-2-yl-radical is the active form of the enzyme
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S-adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine
5'-deoxyadenosine + methionine + flavodoxin + formate acetyltransferase-glycine-2-yl-radical
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the glycyl radical in pyruvate formate-lyase is produced by stereospecific abstraction of the pro-S hydrogen of Gly734 by the 5'-deoxyadenosine radical generated in the active center of the enzyme
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S-adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine
5'-deoxyadenosine + methionine + flavodoxin + formate acetyltransferase-glycine-2-yl-radical
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the interaction with substrate formate C-acetyltransferase is very slow and rate-limited by large conformational changes. The enzyme binds S-adenosyl-L-methionine with the same affinity of about 0.006 mM regardless of the presence or absence of formate C-acetyltransferase. Activation of formate C-acetyltransferase in the presence of its substrate pyruvate or the analogue oxamate results in stoichiometric conversion of the [4Fe-4S]1+ cluster to the glycyl radical on formate C-acetyltransferase, however 3.7-fold less activation is achieved in the absence of these small molecules. Formate C-acetyltransferase, formate C-acetyltransferase activating enzyme, and S-adenosyl-L-methionine are essentially fully bound in vivo, whereas electron donor proteins are partially bound
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5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical
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S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine
5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical
PFL dimer, photoreduced enzyme PFL-AE
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the enzyme also activates an enzyme which has both pyruvate formate-lyase activity and 2-ketobutyrate formate-lyase activity
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additional information
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the enzyme also activates an enzyme which has both pyruvate formate-lyase activity and 2-ketobutyrate formate-lyase activity
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additional information
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a DELTAAla-containing peptide which lacks hydrogens at the 734-Calpha atom is recognized by the enzyme and is able to trap covalently the nucleophilic 5-deoxyadenosine radical
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additional information
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pyruvate formate-lyase-activating enzyme (PFL-AE) activates pyruvate formate-lyase by generating a catalytically essential radical on Gly-734 of pyruvate formate-lyase. PFL-AE shifts the closed/open formation of pyruvate formate-lyase to the open conformation, in which Gly-734 is more solvent-exposed and accessible to the PFL-AE active site
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additional information
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pyruvate formate-lyase-activating enzyme (PFL-AE) activates pyruvate formate-lyase by generating a catalytically essential radical on Gly-734 of pyruvate formate-lyase. PFL-AE shifts the closed/open formation of pyruvate formate-lyase to the open conformation, in which Gly-734 is more solvent-exposed and accessible to the PFL-AE active site
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additional information
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in vivo concentrations of the entire PFL system is calculated to estimate the amount of bound protein in the cell. PFL, PFL-AE, and S-adenosyl-L-methionine are essentially fully bound in vivo, whereas electron donor proteins are partially bound
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additional information
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PFL-AE utilizes S-adenosylmethionine (SAM) and reduced flavodoxin as the cosubstrates to generate a 5'-deoxyadenosyl radical, which then activates PFL by abstracting a hydrogen atom from residue G734
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additional information
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usage of an S-adenosyl-L-methionine binding assay to accurately determine the equilibrium constants for S-adenosyl-L-methionine binding to enzyme PFL-AE alone and in complex with substrate PFL, activation of PFL in the presence of its substrate pyruvate or the analogue oxamate results in stoichiometric conversion of the [4Fe-4S]1+ cluster to the glycyl radical on PFL. 3.7fold less activation is achieved in the absence of these small molecules, demonstrating that pyruvate or oxamate are required for optimal activation. For the assay, the enzyme PFL-AE is attached to a CM5 sensor chip using standard thiol coupling procedures
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