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2-oxobutyrate + CoA
propionyl-CoA + formate
acetyl-CoA + formate
CoA + pyruvate
acetyl-CoA + formate
pyruvate + CoA
CoA + pyruvate
acetyl-CoA + formate
pyruvate + CoA
acetyl-CoA + formate
pyruvate + CoA
formate + acetyl-CoA
pyruvate + dephospho-CoA
dephospho-acetyl-CoA + formate
pyruvate + dithiothreitol
S-acetyl-dithiothreitol + formate
-
-
-
?
pyruvate + formate
formate + pyruvate
pyruvate + phosphate
acetylphosphate + formate
-
-
-
ir
additional information
?
-
2-oxobutyrate + CoA
propionyl-CoA + formate
-
-
-
-
r
2-oxobutyrate + CoA
propionyl-CoA + formate
-
-
-
-
r
2-oxobutyrate + CoA
propionyl-CoA + formate
-
-
-
-
r
acetyl-CoA + formate
CoA + pyruvate
-
-
-
-
?
acetyl-CoA + formate
CoA + pyruvate
-
-
-
-
?
acetyl-CoA + formate
CoA + pyruvate
-
-
-
-
r
acetyl-CoA + formate
CoA + pyruvate
-
-
-
?
acetyl-CoA + formate
CoA + pyruvate
-
-
-
r
acetyl-CoA + formate
CoA + pyruvate
-
-
-
-
r
acetyl-CoA + formate
CoA + pyruvate
-
-
-
-
r
acetyl-CoA + formate
CoA + pyruvate
-
-
-
-
r
acetyl-CoA + formate
CoA + pyruvate
-
-
-
?
acetyl-CoA + formate
CoA + pyruvate
-
-
-
?
acetyl-CoA + formate
pyruvate + CoA
-
-
-
-
r
acetyl-CoA + formate
pyruvate + CoA
-
-
-
-
r
acetyl-CoA + formate
pyruvate + CoA
-
-
-
-
r
acetyl-CoA + formate
pyruvate + CoA
-
-
-
-
r
acetyl-CoA + formate
pyruvate + CoA
-
-
-
r
acetyl-CoA + formate
pyruvate + CoA
-
-
-
-
r
acetyl-CoA + formate
pyruvate + CoA
-
-
-
r
CoA + pyruvate
acetyl-CoA + formate
-
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
-
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
-
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
step in the mitochondrial pathway, overview
-
-
?
CoA + pyruvate
acetyl-CoA + formate
anaerobic metabolism and potential ethanol-producing pathways in Chlamydomonas reinhardtii analyzed
-
-
?
CoA + pyruvate
acetyl-CoA + formate
-
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
-
-
-
-
r
CoA + pyruvate
acetyl-CoA + formate
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
-
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
-
-
-
r
CoA + pyruvate
acetyl-CoA + formate
-
the reaction involves Cys418 and Cys419
-
-
?
CoA + pyruvate
acetyl-CoA + formate
mechanism to truncate an arginine-bound carboxylate motif, substrate mechanism of pyruvate formate-lyase used as a case study
-
-
?
CoA + pyruvate
acetyl-CoA + formate
-
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
-
anaerobic growth under nitrogen, 37°C, pH 7.0, extract enzyme reactions measured at room temperature
-
-
?
CoA + pyruvate
acetyl-CoA + formate
-
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
-
metabolic regulation and networking, overview
-
-
?
CoA + pyruvate
acetyl-CoA + formate
-
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
-
metabolic regulation and networking, overview
-
-
?
CoA + pyruvate
acetyl-CoA + formate
-
-
-
-
r
CoA + pyruvate
acetyl-CoA + formate
-
-
-
-
r
CoA + pyruvate
acetyl-CoA + formate
-
-
-
-
r
CoA + pyruvate
acetyl-CoA + formate
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
formate is an important methyl group donor for anabolic pathway through the formation of folate derivates, formate supply improves Streptococcus thermophilus growth in milk
-
-
?
CoA + pyruvate
acetyl-CoA + formate
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
formate is an important methyl group donor for anabolic pathway through the formation of folate derivates, formate supply improves Streptococcus thermophilus growth in milk
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
-
required for synthesis of C1 units in anabolism
-
-
r
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
-
required for synthesis of C1 units in anabolism
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
required for synthesis of C1 units in anabolism
-
-
r
pyruvate + CoA
acetyl-CoA + formate
-
physiological function is both anabolic and catabolic
-
-
r
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
-
required for synthesis of C1 units in anabolism
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
-
required for synthesis of C1 units in anabolism
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
required for synthesis of C1 units in anabolism
-
-
r
pyruvate + CoA
acetyl-CoA + formate
-
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
required for synthesis of C1 units in anabolism
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
required for synthesis of C1 units in anabolism
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
-
no report on the reverse reaction
-
-
ir, r
pyruvate + CoA
acetyl-CoA + formate
-
catabolic function, leading to production of ATP
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
catabolic function, leading to production of ATP
-
-
ir, r
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
-
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
-
reverse reaction with only 0.1% velocity of the forward reaction
-
-
ir, r
pyruvate + CoA
acetyl-CoA + formate
-
central reaction in the anaerobic metabolism
-
-
r
pyruvate + CoA
acetyl-CoA + formate
-
key enzyme of the glucose fermentation route in anaerobically growing cells
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
key enzyme of the glucose fermentation route in anaerobically growing cells
-
-
r
pyruvate + CoA
acetyl-CoA + formate
key enzyme of the glucose fermentation route in anaerobically growing cells
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
key role in the metabolism
-
-
r
pyruvate + CoA
acetyl-CoA + formate
-
acetyl-CoA for ATP synthesis in catabolism
-
-
ir, r
pyruvate + CoA
acetyl-CoA + formate
-
catabolic function, leading to production of ATP
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
catabolic function, leading to production of ATP
-
-
ir, r
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
-
main enzyme competing for pyruvate under anaerobic conditions
-
-
r
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
catabolic function, leading to production of ATP
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
?, r
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
?, r
pyruvate + CoA
acetyl-CoA + formate
Tequatrovirus T4
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
ir
pyruvate + CoA
acetyl-CoA + formate
-
catabolic function, leading to production of ATP
-
-
ir
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
r
pyruvate + CoA
formate + acetyl-CoA
-
mixed-acid fermentation, necessary for growth in xylose minimal medium under anaerobic conditions
-
-
r
pyruvate + CoA
formate + acetyl-CoA
-
-
-
-
r
pyruvate + dephospho-CoA
dephospho-acetyl-CoA + formate
-
-
-
-
r
pyruvate + dephospho-CoA
dephospho-acetyl-CoA + formate
-
-
-
-
r
pyruvate + dephospho-CoA
dephospho-acetyl-CoA + formate
-
-
-
-
r
pyruvate + formate
formate + pyruvate
-
carboxyl group exchange reaction
-
r
pyruvate + formate
formate + pyruvate
-
carboxyl group exchange reaction
-
r
pyruvate + formate
formate + pyruvate
-
carboxyl group exchange reaction
-
r
pyruvate + formate
formate + pyruvate
-
carboxyl group exchange reaction
-
r
pyruvate + formate
formate + pyruvate
-
carboxyl group exchange reaction
-
r
pyruvate + formate
formate + pyruvate
-
carboxyl group exchange reaction
-
r
pyruvate + formate
formate + pyruvate
-
carboxyl group exchange reaction
-
r
pyruvate + formate
formate + pyruvate
-
carboxyl group exchange reaction
-
r
additional information
?
-
-
the enzyme is a glycyl radical enzyme, changes in the active site indicate that the actual substrate of PFL2 is bigger than a glycerol molecule, but sequence and structural homology suggest that PFL2 may be a dehydratase
-
-
?
additional information
?
-
-
phosphate cannot substitute for CoA
-
-
?
additional information
?
-
-
phosphate cannot substitute for CoA
-
-
?
additional information
?
-
-
phosphate cannot substitute for CoA
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
not essential for nitrate respiration
-
-
?
additional information
?
-
-
The product of yfiD gene is similar to pyruvate formate-lyase activase and it has been reported to activate PFL by replacing the glycyl radical domain, overview, the YfiD protein contributes to the pyruvate formate-lyase flux in the Escherichia coli arcA mutant strain, but not in the wild-type strain
-
-
?
additional information
?
-
pyruvate formate-lyase interacts directly with the formate channel FocA to regulate formate translocation, molecular modeling of the FocA-PflB complex, the N-terminus of FocA is important for interaction with enzyme PflB
-
-
?
additional information
?
-
-
pyruvate formate-lyase interacts directly with the formate channel FocA to regulate formate translocation, molecular modeling of the FocA-PflB complex, the N-terminus of FocA is important for interaction with enzyme PflB
-
-
?
additional information
?
-
formate channel FocA interacts with inactive PflB in vitro, analysis by mixing equal amounts of purified Strep-tagged FocA and purified His-tagged PflB, cross-links between FocA and PflBare identified, detailed overview
-
-
?
additional information
?
-
-
formate channel FocA interacts with inactive PflB in vitro, analysis by mixing equal amounts of purified Strep-tagged FocA and purified His-tagged PflB, cross-links between FocA and PflBare identified, detailed overview
-
-
?
additional information
?
-
pyruvate formate lyase (PFL) is characterized as an enzyme functional at anaerobic conditions, since the radical in the enzyme's active form is sensitive to oxygen
-
-
?
additional information
?
-
-
pyruvate formate lyase (PFL) is characterized as an enzyme functional at anaerobic conditions, since the radical in the enzyme's active form is sensitive to oxygen
-
-
?
additional information
?
-
-
hydrogen is formed from pyruvate by multiple parallel pathways, one pathway involves formate as an intermediate, pyruvate-formate lyase, and formate-hydrogen lyase, comprised of HydA hydrogenase and formate dehydrogenase, and a formate-independent pathway involving pyruvate dehydrogenase, the expression of pflB paralleled the expression of hydA and hyaB
-
-
?
additional information
?
-
-
hydrogen is formed from pyruvate by multiple parallel pathways, one pathway involves formate as an intermediate, pyruvate-formate lyase, and formate-hydrogen lyase, comprised of HydA hydrogenase and formate dehydrogenase, and a formate-independent pathway involving pyruvate dehydrogenase, the expression of pflB paralleled the expression of hydA and hyaB
-
-
?
additional information
?
-
analysis of the cytosolic proteome involving the enzyme, proteome profile
-
-
?
additional information
?
-
-
analysis of the cytosolic proteome involving the enzyme, proteome profile
-
-
?
additional information
?
-
analysis of the cytosolic proteome involving the enzyme, proteome profile
-
-
?
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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 butyricum, Clostridium kluyveri, Clostridium pasteurianum, Clostridium pasteurianum (Q46266), Clostridium sp., Escherichia coli, Enterococcus faecalis, no activity in Clostridium pasteurianum, Streptococcus mutans, Streptococcus salivarius, Streptococcus sanguinis, Clostridium pasteurianum DSM 525, Clostridium butyricum DSM 552, Streptococcus sanguinis DSM 20066
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
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, Streptococcus mutans
brenda
Rdel, 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
Thauer, R.K.; Kirchniawy, F.H.; Jungermann, K.A.
Properties and function of the pyruvate-formate-lyase reaction in clostridiae
Eur. J. Biochem.
27
282-290
1972
Clostridium beijerinckii, Clostridium butyricum, Clostridium kluyveri, Clostridium sp., Escherichia coli, Enterococcus faecalis, Veillonella parvula, no activity in Clostridium pasteurianum
brenda
Wood, N.P.; Jungermann, K.
Inactivation of the pyruvate formate lyase of Clostridium butyricum
FEBS Lett.
27
49-52
1972
Clostridium butyricum, Escherichia coli, Enterococcus faecalis
brenda
Knappe, J.; Balschkowski, H.P.; Grbner, P.; Schmitt, T.
Pyruvate formate-lyase of Escherichia coli: the acetyl-enzyme intermediate
Eur. J. Biochem.
50
253-263
1974
Escherichia coli
brenda
Knappe, J.; Blaschkowski, H.P.
Pyruvate formate-lyase from Escherichia coli and its activation system
Methods Enzymol.
41B
508-518
1975
Clostridium sp., Escherichia coli, Enterococcus faecalis
-
brenda
Takahashi, S.; Abbe, K.; Yamada, T.
Purification of pyruvate formate-lyase from Streptococcus mutans and its regulatory properties
J. Bacteriol.
149
1034-1040
1982
Clostridium butyricum, Clostridium sp., Escherichia coli, Enterococcus faecalis, Lactobacillus delbrueckii subsp. bulgaricus, Lactococcus lactis, Streptococcus mutans, Streptococcus mutans JC2
brenda
Ulissi-DeMario, L.; Brush, E.J.; Kozarich, J.W.
Mechanism-based inactivation of pyruvate formate-lyase reaction in Clostridiae
J. Am. Chem. Soc.
113
4341-4342
1991
Escherichia coli
-
brenda
Wagner, A.F.V.; Frey, M.; Neugebauer, F.A.; Schfer, W.; Knappe, J.
The free radical in pyruvate formate-lyase is located on glycine-734
Proc. Natl. Acad. Sci. USA
89
996-1000
1992
Escherichia coli
brenda
Knappe, J.; Elbert, S.; Frey, M.; Wagner, A.F.V.
Pyruvate formate-lyase mechanism involving the protein-based glycyl radical
Biochem. Soc. Trans.
21
731-734
1993
Escherichia coli
-
brenda
Kaiser, M.; Sawers, G.
Pyruvate formate-lyase is not essential for nitrate respiration by Escherichia coli
FEMS Microbiol. Lett.
117
163-168
1994
Escherichia coli
brenda
Broderick, J.B.; Duderstadt, R.E.; Fernandez, D.C.; Wojtuszewski, K.; Henshaw, T.F.; Johnson, M.K.
Pyruvate formate-lyase activating enzyme is an iron-sulfur protein
J. Am. Chem. Soc.
119
7396-7397
1997
Escherichia coli
-
brenda
Himo, F.; Eriksson, L.A.
Catalytic mechanism of pyruvate formate-lyase (PFL). A theoretical study
J. Am. Chem. Soc.
120
11449-11455
1998
Escherichia coli
-
brenda
Becker, A.; Fritz-Wolf, K.; Kabsch, W.; Knappe, J.; Schultz, S.; Wagner, A.F.V.
Structure and mechanism of the glycyl radical enzyme pyruvate formate-lyase
Nat. Struct. Biol.
6
969-975
1999
Escherichia coli, Escherichia coli (P09373)
brenda
Asanuma, N.; Hino, T.
Effects of pH and energy supply on activity and amount of pyruvate formate-lyase in Streptococcus bovis
Appl. Environ. Microbiol.
66
3773-3777
2000
Clostridium butyricum, Escherichia coli, Lactococcus lactis, Streptococcus equinus, Streptococcus mutans
brenda
Wagner, A.F.V.; Schultz, S.; Bomke, J.; Pils, T.; Lehmann, W.D.; Knappe, J.
YfiD of Escherichia coli and Y06I of bacteriophage T4 as autonomous glycyl radical cofactors reconstituting the catalytic center of oxygen-fragmented pyruvate formate-lyase
Biochem. Biophys. Res. Commun.
285
456-462
2001
Tequatrovirus T4, Escherichia coli, Escherichia coli (P09373), Haemophilus influenzae, Pasteurella multocida, Yersinia pestis, Salmonella enterica subsp. enterica serovar Typhimurium, Vibrio cholerae serotype O1
brenda
Zhang, W.; Wong, K.K.; Magliozzo, R.S.; Kozarich, J.W.
Inactivation of pyruvate formate-lyase by dioxygen: Defining the mechanistic interplay of glycine 734 and cysteine 419 by rapid freeze-quench EPR
Biochemistry
40
4123-4130
2001
Escherichia coli
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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
Clostridium pasteurianum, Escherichia coli, Lactococcus lactis, Streptococcus equinus, Streptococcus equinus (O66391)
brenda
Becker, A.; Kabsch, W.
X-ray structure of pyruvate formate-lyase in complex with pyruvate and CoA. How the enzyme uses the Cys-418 thiyl radical for pyruvate cleavage
J. Biol. Chem.
277
40036-40042
2002
Escherichia coli (P09373)
brenda
Lehtioe, L.; Leppaenen, V.M.; Kozarich, J.W.; Goldman, A.
Structure of Escherichia coli pyruvate formate-lyase with pyruvate
Acta Crystallogr. Sect. D
58
2209-2212
2002
Escherichia coli (P09373), Escherichia coli
brenda
Melchiorsen, C.R.; Jokumsen, K.V.; Villadsen, J.; Israelsen, H.; Arnau, J.
The level of pyruvate-formate lyase controls the shift from homolactic to mixed-acid product formation in Lactococcus lactis
Appl. Microbiol. Biotechnol.
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338-344
2002
Escherichia coli, Lactococcus lactis
brenda
Hasona, A.; Kim, Y.; Healy, F.G.; Ingram, L.O.; Shanmugam, K.T.
Pyruvate formate lyase and acetate kinase are essential for anaerobic growth of Escherichia coli on xylose
J. Bacteriol.
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7593-7600
2004
Escherichia coli
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Plaga, W.; Vielhaber, G.; Wallach, J.; Knappe, J.
Modification of Cys-418 of pyruvate format-lyase by methacrylic acid, based on its radical mechanism
FEBS Lett.
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2000
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 (Q6RFH7), Neocallimastix frontalis
brenda
De Lucas, M.; Fernandes, P.A.; Eriksson, L.A.; Ramos, M.J.
Pyruvate formate lyase: a new perspective
J. Phys. Chem. B
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2003
Escherichia coli
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brenda
Boxma, B.; Voncken, F.; Jannink, S.; van Alen, T.; Akhmanova, A.; van Weelden, S.W.; van Hellemond, J.J.; Ricard, G.; Huynen, M.; Tielens, A.G.; Hackstein, J.H.
The anaerobic chytridiomycete fungus Piromyces sp. E2 produces ethanol via pyruvate:formate lyase and an alcohol dehydrogenase E
Mol. Microbiol.
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1389-1399
2004
Piromyces sp. E2
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.
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293-297
2003
Streptococcus mutans
brenda
Derzelle, S.; Bolotin, A.; Mistou, M.Y.; Rul, F.
Proteome analysis of Streptococcus thermophilus grown in milk reveals pyruvate formate-lyase as the major upregulated protein
Appl. Environ. Microbiol.
71
8597-8605
2005
Streptococcus thermophilus (Q5M2Y4), Streptococcus thermophilus, Streptococcus thermophilus LMG18311 (Q5M2Y4)
brenda
Meshulam-Simon, G.; Behrens, S.; Choo, A.D.; Spormann, A.M.
Hydrogen metabolism in Shewanella oneidensis MR-1
Appl. Environ. Microbiol.
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1153-1165
2007
Shewanella oneidensis, Shewanella oneidensis MR-1 / ATCC 700550
brenda
Nnyepi, M.R.; Peng, Y.; Broderick, J.B.
Inactivation of E. coli pyruvate formate-lyase: role of AdhE and small molecules
Arch. Biochem. Biophys.
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2007
Escherichia coli
brenda
Yang, D.F.; Wei, Y.T.; Huang, R.B.
Computer-aided design of the stability of pyruvate formate-lyase from Escherichia coli by site-directed mutagenesis
Biosci. Biotechnol. Biochem.
71
746-753
2007
Escherichia coli, Escherichia coli JM109
brenda
Zhu, J.; Shalel-Levanon, S.; Bennett, G.; San, K.Y.
The YfiD protein contributes to the pyruvate formate-lyase flux in an Escherichia coli arcA mutant strain
Biotechnol. Bioeng.
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2007
Escherichia coli
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.
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2006
Acetivibrio thermocellus
brenda
Lucas, M.d.e.F.; Ramos, M.J.
Theoretical study of the suicide inhibition mechanism of the enzyme pyruvate formate lyase by methacrylate
J. Am. Chem. Soc.
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2005
Escherichia coli
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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.
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Chlamydomonas reinhardtii (Q1RS83), Chlamydomonas reinhardtii
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Lehtioe, L.; Grossmann, J.G.; Kokona, B.; Fairman, R.; Goldman, A.
Crystal structure of a glycyl radical enzyme from Archaeoglobus fulgidus
J. Mol. Biol.
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Archaeoglobus fulgidus
brenda
Hemschemeier, A.; Jacobs, J.; Happe, T.
Biochemical and physiological characterization of the pyruvate formate-lyase Pfl1 of Chlamydomonas reinhardtii, a typically bacterial enzyme in a eukaryotic alga
Eukaryot. Cell
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518-526
2008
Chlamydomonas reinhardtii (P37836), Chlamydomonas reinhardtii
brenda
Condic-Jurkic, K.; Perchyonok, V.T.; Zipse, H.; Smith, D.M.
On the modeling of arginine-bound carboxylates: A case study with Pyruvate Formate-Lyase
J. Comput. Chem.
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2008
Escherichia coli (P09373)
brenda
Wang, Q.; Ou, M.S.; Kim, Y.; Ingram, L.O.; Shanmugam, K.T.
Metabolic Flux Control at the Pyruvate Node in an Anaerobic Escherichia coli with Active Pyruvate Dehydrogenase
Appl. Environ. Microbiol.
76
2107-2114
2010
Escherichia coli str. K-12 substr. W3110
brenda
Yesilkaya, H.; Spissu, F.; Carvalho, S.M.; Terra, V.S.; Homer, K.A.; Benisty, R.; Porat, N.; Neves, A.R.; Andrew, P.W.
Pyruvate formate lyase is required for pneumococcal fermentative metabolism and virulence
Infect. Immun.
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2009
Streptococcus pneumoniae D39
brenda
Utrilla, J.; Gosset, G.; Martinez, A.
ATP limitation in a pyruvate formate lyase mutant of Escherichia coli MG1655 increases glycolytic flux to D-lactate
J. Ind. Microbiol. Biotechnol.
36
1057-1062
2009
Escherichia coli str. K-12 substr. MG1655
brenda
Leibig, M.; Liebeke, M.; Mader, D.; Lalk, M.; Peschel, A.; Goetz, F.
Pyruvate formate lyase acts as a formate supplier for metabolic processes during anaerobiosis in Staphylococcus aureus
J. Bacteriol.
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2011
Staphylococcus aureus
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Crain, A.V.; Broderick, J.B.
Pyruvate formate-lyase and its activation by pyruvate formate-lyase activating enzyme
J. Biol. Chem.
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2013
Escherichia coli (P09373)
brenda
Zhou, J.; Olson, D.; Lanahan, A.; Tian, L.; Murphy, S.; Lo, J.; Lynd, L.
Physiological roles of pyruvate ferredoxin oxidoreductase and pyruvate formate-lyase in Thermoanaerobacterium saccharolyticum JW/SL-YS485
Biotechnol. Biofuels
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138
2015
Thermoanaerobacterium saccharolyticum (I3VT07), Thermoanaerobacterium saccharolyticum, Thermoanaerobacterium saccharolyticum DSM 8691 (I3VT07)
brenda
Zhang, Y.; Dai, Z.; Krivoruchko, A.; Chen, Y.; Siewers, V.; Nielsen, J.
Functional pyruvate formate lyase pathway expressed with two different electron donors in Saccharomyces cerevisiae at aerobic growth
FEMS Yeast Res.
15
fov024
2015
Escherichia coli (P09373), Escherichia coli
brenda
Khelifi, N.; Amin Ali, O.; Roche, P.; Grossi, V.; Brochier-Armanet, C.; Valette, O.; Ollivier, B.; Dolla, A.; Hirschler-Rea, A.
Anaerobic oxidation of long-chain n-alkanes by the hyperthermophilic sulfate-reducing archaeon, Archaeoglobus fulgidus
ISME J.
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2153-2166
2014
Archaeoglobus fulgidus (O28823), Archaeoglobus fulgidus
brenda
Doi, Y.; Ikegami, Y.
Pyruvate formate-lyase is essential for fumarate-independent anaerobic glycerol utilization in the Enterococcus faecalis strain W11
J. Bacteriol.
196
2472-2480
2014
Enterococcus faecalis, Enterococcus faecalis W11
brenda
Doberenz, C.; Zorn, M.; Falke, D.; Nannemann, D.; Hunger, D.; Beyer, L.; Ihling, C.H.; Meiler, J.; Sinz, A.; Sawers, R.G.
Pyruvate formate-lyase interacts directly with the formate channel FocA to regulate formate translocation
J. Mol. Biol.
426
2827-2839
2014
Escherichia coli (P09373), Escherichia coli
brenda
Zhang, Y.; Dai, Z.; Krivoruchko, A.; Chen, Y.; Siewers, V.; Nielsen, J.
Functional pyruvate formate lyase pathway expressed with two different electron donors in Saccharomyces cerevisiae at aerobic growth
FEMS Yeast Res.
15
fov024
2015
Escherichia coli (P09373), Escherichia coli
brenda
Crain, A.; Broderick, J.
Pyruvate formate-lyase and its activation by pyruvate formate-lyase activating enzyme
J. Biol. Chem.
289
5723-5729
2014
Escherichia coli (P09373)
brenda
Al-Bayati, F.A.; Kahya, H.F.; Damianou, A.; Shafeeq, S.; Kuipers, O.P.; Andrew, P.W.; Yesilkaya, H.
Pneumococcal galactose catabolism is controlled by multiple regulators acting on pyruvate formate lyase
Sci. Rep.
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43587
2017
Streptococcus pneumoniae (A0A0H2ZQE4), Streptococcus pneumoniae
brenda
Zelcbuch, L.; Lindner, S.N.; Zegman, Y.; Vainberg Slutskin, I.; Antonovsky, N.; Gleizer, S.; Milo, R.; Bar-Even, A.
Pyruvate formate-lyase enables efficient growth of Escherichia coli on acetate and formate
Biochemistry
55
2423-2426
2016
Escherichia coli
brenda
Hanzevacki, M.; Condic-Jurkic, K.; Banhatti, R.D.; Smith, A.S.; Smith, D.M.
The influence of chemical change on protein dynamics a case study with pyruvate formate-lyase
Chemistry
25
8741-8753
2019
Escherichia coli (P09373)
brenda
Hanzevacki, M.; Banhatti, R.D.; Condic-Jurkic, K.; Smith, A.S.; Smith, D.M.
Exploring reactive conformations of coenzyme A during binding and unbinding to pyruvate formate-lyase
J. Phys. Chem. A
123
9345-9356
2019
Escherichia coli (P09373)
brenda
Kim, S.; Lee, J.; Lee, S.; Ha, J.; Lee, J.; Choi, Y.; Oh, H.; Yoon, Y.; Choi, K.
Invasion of intestinal cells by Staphylococcus aureus is mediated by pyruvate formate lyase (Pfl) protein
J. Pure Appl. Microbiol.
13
647-652
2019
Staphylococcus aureus, Staphylococcus aureus NCCP10862, Staphylococcus aureus KACC10768
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brenda
Byer, A.S.; McDaniel, E.C.; Impano, S.; Broderick, W.E.; Broderick, J.B.
Mechanistic studies of radical SAM enzymes pyruvate formate-lyase activating enzyme and lysine 2,3-aminomutase case studies
Methods Enzymol.
606
269-318
2018
Escherichia coli
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