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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 + 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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additional information
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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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-
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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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-
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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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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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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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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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C102S
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mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent
C12S
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mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent
C29S
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mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent
C33S
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mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent
C36S
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mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent
C94S
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mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent
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Johnson, M.K.; Staples, C.R.; Duin, E.C.; Lafferty, M.E.; Duderstadt, R.E.
Novel roles for Fe-S clusters in stabilizing or generating radical intermediates
Pure Appl. Chem.
70
939-946
1998
Escherichia coli
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brenda
Weidner, G.; Sawers, G.
Molecular characterization of the genes encoding pyruvate formate-lyase and its activating enzyme of Clostridium pasteurianum
J. Bacteriol.
178
2440-2444
1996
Clostridium pasteurianum
brenda
Kulzer, R.; Pils, T.; Kappl, R.; Huttermann, J.; Knappe, J.
Reconstitution and characterization of the polynuclear iron-sulfur cluster in pyruvate formate-lyase-activating enzyme. Molecular properties of the holoenzyme form
J. Biol. Chem.
273
4897-4903
1998
Escherichia coli
brenda
Frey, M.; Rothe, M.; Wagner, A.F.V.; Knappe, J.
Adenosylmethionine-dependent synthesis of the glycyl radical in pyruvate formate-lyase by abstraction of the glycine C-2 pro-S hydrogen atom
J. Biol. Chem.
269
12432-12437
1994
Escherichia coli
brenda
Wong, K.K.; Murray, B.W.; Lewisch, S.A.; Baxter, M.K.; Ridky, T.W.; Ulissi-DeMario, L.; Kozarich, J.W.
Molecular properties of pyruvate formate-lyase activating enzyme
Biochemistry
32
14102-14110
1993
Escherichia coli
brenda
Wagner, A.F.V.; Demand, J.; Schilling, G.; Pils, T.; Knappe, J.
A dehydroalanyl residue can capture the 5'-deoxyadenosyl radical generated from S-adenosylmethionine by pyruvate formate-lyase-activating enzyme
Biochem. Biophys. Res. Commun.
254
306-310
1999
Escherichia coli
brenda
Conradt, H.; Hohmann-Berger, M.; Hohmann, H.P.; Blaschkowski, H.P.; Knappe, J.
Pyruvate formate-lyase (inactive form) and pyruvate formate-lyase activating enzyme of Escherichia coli: isolation and structural properties
Arch. Biochem. Biophys.
228
133-142
1984
Escherichia coli
brenda
Rödel, W.; Plaga, W.; Frank, W.; Knappe, J.
Primary structures of Escherichia coli pyruvate formate-lyase and pyruvate-formate-lyase-activating enzyme deduced from the DNA nucleotide sequences
Eur. J. Biochem.
177
153-158
1988
Escherichia coli
brenda
Sawers, G.; Watson, G.
A glycyl radical solution: oxygen-dependent interconversion of pyruvate formate-lyase
Mol. Microbiol.
29
945-954
1998
Escherichia coli
brenda
Hesslinger, C.; Fairhurst, S.A.; Sawers, G.
Novel keto acid formate-lyase and propionate kinase enzynes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate
Mol. Microbiol.
27
477-492
1998
Escherichia coli
brenda
Asanuma, N.; Hino, T.
Molecular characterization and expression of pyruvate formate-lyase-activating enzyme in a ruminal bacterium, Streptococcus bovis
Appl. Environ. Microbiol.
68
3352-3357
2002
Streptococcus equinus (Q93UQ7), Streptococcus equinus
brenda
Broderick, J.B.; Henshaw, T.F.; Cheek, J.; Wojtuszewski, K.; Smith, S.R.; Trojan, M.R.; McGhan, R.M.; Kopf, A.; Kibbey, M.; Broderick, W.E.
Pyruvate formate-lyase-activating enzyme: Strictly anaerobic isolation yields active enzyme containing a [3Fe-4S]+ cluster
Biochem. Biophys. Res. Commun.
269
451-456
2000
Escherichia coli
brenda
Krebs, C.; Broderick, W.E.; Henshaw, T.F.; Broderick, J.B.; Huynh, B.H.
Coordination of adenosylmethionine to a unique iron site of the [4Fe-4S] of pyruvate formate-lyase activating enzyme: a moessbauer spectroscopic study
J. Am. Chem. Soc.
124
912-913
2002
Escherichia coli
brenda
Gelius-Dietrich, G.; Henze, K.
Pyruvate formate lyase (PFL) and PFL activating enzyme in the chytrid fungus Neocallimastix frontalis: a free-radical enzyme system conserved across divergent eukaryotic lineages
J. Eukaryot. Microbiol.
51
456-463
2004
Neocallimastix frontalis, Neocallimastix frontalis (Q6RFH6)
brenda
Takahashi-Abbe, S.; Abe, K.; Takahashi, N.
Biochemical and functional properties of a pyruvate formate-lyase (PFL)-activating system in Streptococcus mutans
Oral Microbiol. Immunol.
18
293-297
2003
Streptococcus mutans
brenda
Sparling, R.; Islam, R.; Cicek, N.; Carere, C.; Chow, H.; Levin, D.B.
Formate synthesis by Clostridium thermocellum during anaerobic fermentation
Can. J. Microbiol.
52
681-688
2006
Ruminiclostridium thermocellum, Ruminiclostridium thermocellum 27405.
brenda
Atteia, A.; van Lis, R.; Gelius-Dietrich, G.; Adrait, A.; Garin, J.; Joyard, J.; Rolland, N.; Martin, W.
Pyruvate formate-lyase and a novel route of eukaryotic ATP synthesis in Chlamydomonas mitochondria
J. Biol. Chem.
281
9909-9918
2006
Chlamydomonas reinhardtii
brenda
Peng, Y.; Veneziano, S.E.; Gillispie, G.D.; Broderick, J.B.
Pyruvate formate-lyase, evidence for an open conformation favored in the presence of its activating enzyme
J. Biol. Chem.
285
27224-27231
2010
Escherichia coli, Escherichia coli (P0A9N4)
brenda
Crain, A.V.; Broderick, J.B.
Flavodoxin cofactor binding induces structural changes that are required for protein-protein interactions with NADP(+) oxidoreductase and pyruvate formate-lyase activating enzyme
Biochim. Biophys. Acta
1834
2512-2519
2013
Escherichia coli
brenda
Dey, A.; Peng, Y.; Broderick, W.E.; Hedman, B.; Hodgson, K.O.; Broderick, J.B.; Solomon, E.I.
S K-edge XAS and DFT calculations on SAM dependent pyruvate formate-lyase activating enzyme: nature of interaction between the Fe4S4 cluster and SAM and its role in reactivity
J. Am. Chem. Soc.
133
18656-18662
2011
Escherichia coli
brenda
Crain, A.V.; Broderick, J.B.
Pyruvate formate-lyase and its activation by pyruvate formate-lyase activating enzyme
J. Biol. Chem.
289
5723-5729
2013
Escherichia coli
brenda