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Information on EC 2.3.1.54 - formate C-acetyltransferase and Organism(s) Escherichia coli and UniProt Accession P09373
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2.3.1.54 formate C-acetyltransferaseSpecify your search results
Word Map
- 2.3.1.54
-
glycyl
- anaerobiosis
- phosphotransacetylase
-
chemostats
-
homolactic
-
glucose-limited
-
microaerobic
-
pyruvate:ferredoxin
-
mixed-acid
- acetoin
- flavodoxins
- activase
-
5\'-deoxyadenosyl
-
dual-phase
- hypophosphite
-
knappe
- benzylsuccinate
-
embden-meyerhof-parnas
- biotechnology
- nutrition
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
pyruvate formate-lyase, pyruvate formate lyase, pyruvate-formate lyase, pyruvate:formate lyase, formate acetyltransferase, phosphotransferase system enzyme i, formate c-acetyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PFL I
formate acetyltransferase
-
-
-
-
PFL
-
-
pyruvate formate-lyase
pyruvic formate-lyase
-
-
-
-
pyruvate formate-lyase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + formate = CoA + pyruvate
modelling study proposes a four-step mechanism. The reaction is initiated by H transfer from C418 via C410 to the glycyl radical G734. H transfer from C419 to G734 is the rate-limiting process
-
acetyl-CoA + formate = CoA + pyruvate
catalytic mechanism involving residues Gly734, Cys418 and Cys419, transition state, modeling, overview
-
acetyl-CoA + formate = CoA + pyruvate
the reaction mechanism proceeds via generation of a catalytically essential glycyl radical at Gly734
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:formate C-acetyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY
9068-08-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pyruvate + CoA
formate + acetyl-CoA
-
mixed-acid fermentation, necessary for growth in xylose minimal medium under anaerobic conditions
-
-
r
CoA + pyruvate
acetyl-CoA + formate
mechanism to truncate an arginine-bound carboxylate motif, substrate mechanism of pyruvate formate-lyase used as a case study
-
-
?
pyruvate + CoA
acetyl-CoA + formate
key enzyme of the glucose fermentation route in anaerobically growing cells
-
-
?
CoA + pyruvate
acetyl-CoA + formate
-
the reaction involves Cys418 and Cys419
-
-
?
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
-
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 + formate
formate + pyruvate
-
carboxyl group exchange reaction
-
r
pyruvate + formate
formate + pyruvate
-
carboxyl group exchange reaction
-
r
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
?
-
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pyruvate + CoA
formate + acetyl-CoA
-
mixed-acid fermentation, necessary for growth in xylose minimal medium under anaerobic conditions
-
-
r
pyruvate + CoA
acetyl-CoA + formate
key enzyme of the glucose fermentation route in anaerobically growing cells
-
-
?
pyruvate + CoA
acetyl-CoA + formate
-
-
-
-
?
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
-
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
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
?
-
-
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
[4Fe-4S]-center
the [4Fe-4S] cluster of enzyme PFL-AE is coordinated by the cysteines of a conserved CX3CX2C motif, with the fourth unique iron coordinated by S-adenosyl-L-methionine. PFL-AE contains six cysteine residues (Cys12, Cys29, Cys33, Cys36, Cys94, Cys102) and only Cys29, Cys33, and Cys36 are involved in coordinating the iron sulfur cluster
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
rapid, reversible inactivation, deactivation is a non-destructive transfer of an H atom equivalent to quench the glycyl radical
DTT
-
reversible inactivation, deactivation is a non-destructive transfer of an H atom equivalent to quench the glycyl radical
additional information
-
the putative pyruvate formate-lyase deactivase, as activity of AdhE together with an alcohol dehydrogenase and an acetaldehyde-CoA dehydrogenase activities, is not active on the enzyme PFL, it has no PFL deactivating activity
-
methacrylate
-
suicide inhibition mechanism, possibly involving also Arg176 and Arg435, binds to Cys419, modeling, overview
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyruvate formate lyase activating enzyme
activates the enzyme by forming a glycine radical, cf. EC 1.97.1.4
-
pyruvate formate-lyase activating enzyme
-
converts the enzyme to its catalytically active state by generating a stable glycyl radical in the active site at G734
-
YfiD
autonomous glycyl radical cofactor, reconstituting the catalytic center of oxygen-fragmented enzyme
-
pyruvate formate-lyase activating enzyme
PFL-AE, EC 1.97.1.4, pyruvate formate-lyase is a glycyl radical enzyme activated by a radical AdoMet-activating enzyme PFL-AE, that exists largely in complex with enzyme PFL and S-adenosyl-L-methionine, all fully bound. Activation of pyruvate formate-lyase by pyruvate formate-lyase activating enzyme involves formation of a specific glycyl radical on pyruvate formate-lyase by the pyruvate formate-lyase activating enzyme in a reaction requiring S-adenosyl-L-methionine. 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 PF, 3.7fold less activation is achieved in the absence of these small molecules, demonstrating that pyruvate or oxamate are required for optimal activation. The [4Fe-4S] cluster of PFL-AE is coordinated by the cysteines of a conserved CX3CX2C motif, with the fourth unique iron coordinated by S-adenosyl-L-methionine. PFL-AE cycles between two different oxidation states during hydrogen abstraction, [4Fe-4S]2+/1+, with the [4Fe-4S]1+ being the state capable of reductive cleavage of AdoMet to generate the glycyl radical
-
pyruvate formate-lyase activating enzyme
PflA, the enzyme is required to convert pyruvate formate-lyase, PflB, from its inactive to its active, glycyl-radical-containing species
-
pyruvate formate-lyase activating enzyme
PFL-AE, EC 1.97.1.4, 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. 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. PFL activation studies, binding kinetics, overview
-
S-adenosylmethionine
-
obligatory component of the activation reaction
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetics and equilibrium constant for the enzyme's interaction with activating enzyme PFL-AE, the interaction is very slow and rate-limited by large conformational changes, circular dichroism study
-
additional information
additional information
-
steady-state kinetics of wild-type and mutant enzymes
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
mechanistic effect of choosing different protonation states for a substrate carboxylate group that is involved in a salt bridge with an arginine residue analyzed, modeling of arginine-bound carboxylates, computational details, neutral model and anionic model presented, extended model consists of pyruvate in a complex with methylguanidinum and methylthiyl radical, neutral carboxylic acid as a more realistic approximation to the salt bridge arrangement than a bare anionic carboxylate substituent
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PFL wild-type, structure factor amplitude and model coordinate, Protein Data Bank accession code
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
microaerobic cultures, glucose-limited chemostat cultures, different strains, growth rates, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the normally soluble dimeric enzyme pyruvate formate-lyase (PflB) interacts specifically with FocA, association of PflB with the cytoplasmic membrane is FocA-dependent
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
metabolism
physiological function
enzyme pyruvate formate-lyase is responsible for intracellular formate generation in enterobacteria and other microbes
physiological function
pyruvate formate lyase (PFL) forms an alternative pathway for acetyl-CoA biosynthesis. Pyruvate formate lyase is characterized as an enzyme functional at anaerobic conditions, since the radical in the enzyme's active form is sensitive to oxygen. PFL pathway can be functional at aerobic growth conditions in yeast when coexpressed with appropriate electron donors
physiological function
pyruvate formate-lyase (PFL) supplies the citric acid cycle with acetyl-CoA during anaerobic glycolysis by catalyzing the formation of acetyl-CoA and formate from CoA and pyruvate, and is a central enzyme in anaerobic metabolism of Escherichia coli and other facultative anaerobes. PFL is a glycyl radical enzyme, which play key roles in anaerobic metabolism in microbes, including the reduction of ribonucleotides to deoxyribonucleotides, synthesis of benzylsuccinate, and conversion of choline to trimethylamine
metabolism
-
the enzyme can serve as a sole route for microbial growth on acetate and formate
metabolism
-
the enzyme catalyzes the conversion of pyruvate and CoA to formate and acetyl-CoA during anaerobic glucose metabolism
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
85000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
space group P4(3)2(1)2, cell parameters a = b = 158.36 A, c = 159.30 A
structure of the pyruvate formate-lyase monomer in complex with pyruvate and CoA, structure of active site, small model computational studies of the pyruvate formate-lyase substrate transformation
tetragonal crystals in complex with pyruvate, monoclinic cocrystals with CoA and either pyruvate or oxamate obtained by hanging drop method, space group C222_1, a = 54.90 A, b = 153.05 A, c = 205.95
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A273C
-
site-directed mutagenesis, the mutant is less thermostable than the wild-type enzyme
E336C
-
site-directed mutagenesis, the mutant is more thermostable than the wild-type enzyme, Tm is increased 3.7fold, half-life 1.8fold
E400I
-
site-directed mutagenesis, the mutant is more thermostable than the wild-type enzyme, Tm is increased 2.2fold, half-life 2.21fold
additional information
additional information
deletion of both pflA and pflB (strain RM220) partially restores the ability of the strain to respond to exogenous formate
additional information
-
deletion of both pflA and pflB (strain RM220) partially restores the ability of the strain to respond to exogenous formate
additional information
recombinant coexpression of the enzyme with pyruvate format lyase activating enzyme and flavodoxin or ferredoxin in Saccharomyces cerevisiae leads to over 20fold increased expression of endogenous formate dehydrogenases FDH1 and FDH2
additional information
-
recombinant coexpression of the enzyme with pyruvate format lyase activating enzyme and flavodoxin or ferredoxin in Saccharomyces cerevisiae leads to over 20fold increased expression of endogenous formate dehydrogenases FDH1 and FDH2
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 30
-
stable in anaerobic buffers for days at 0°C, at 30°C for several hours
30
30
-
pH 7.5, half-lives of recombinant wild-type and mutant enzymes, overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
virtually stable at 0°C and pH 8.0 if kept in media which display a redoxpotential of 0.2 V or below
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
extreme sensitivity towards inactivation by oxygen, admittance of oxygen inactivates completely within a few seconds
-
487220, 487221
obligate anaerobic enzyme, enzymatic conversion by a unique homolytic mechanism that involves a free radical harbored in the protein structure, protein based organic free radical is essential for catalysis, oxygen destruction of the protein radical
-
487225, 487226, 487236
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 10 mM MOPS-KOH, pH 7.0, 50 mM KCl, thiols, EDTA in 50% ethyleneglycol, proved stable for months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from strain BL21(DE3) by gel filtration and anion exchange chromatography, recombinant His6-tagged enzyme from strain BL21(DE3) by nickel affinity chromatography as single enzyme or as AdhE-Pfl
-
quaternary methylamine AP5-ion exchange column chromatography and phenyl Sepharose column chromatography
-
recombinant His-tagged wild-type and mutant enzymes from strain BL21(DE3) by nickel affinity chromatography to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene pflB, coexpression of pyruvate formate lyase with the pyruvate formate lyase activating enzyme (gene pflA, UniProt ID P0A9N4) as well as with appropriate electron donors flavodoxin and ferredoxin (encoded by genes fldA and fdx, respectively), in a non-ethanol-producing Saccharomyces cerevisiae strain IMI076 lacking pyruvate decarboxylase and having a reduced glucose uptake rate due to a mutation in the transcriptional regulator Mth1, IMI076 (Pdc- MTH1-DELTAT ura3-52), plasmid maps, overview. Reduced flavodoxin is the preferred electron donor, but coexpression of either of the electron donors has a positive effect on growth under aerobic conditions. Subcloning in Escherichia coli strain DH5alpha. The PFL pathway can be functional at aerobic growth conditions in yeast when coexpressed with appropriate electron donors
gene pflB, overexpression of the enzyme from plasmid 29 in the soluble fraction of Escherichia coli strain MC4100
gene pflB, the enzyme and its activating enzyme from Escherichia coli are expressed in a Saccharomyces cerevisiae strain IMI076 lacking pyruvate decarboxylase and having a reduced glucose uptake rate due to a mutation in the transcriptional regulator Mth1. Enzyme PFL is expressed with two different electron donors, reduced ferredoxin or reduced flavodoxin, respectively. The coexpression of either of these electron donors has a positive effect on growth under aerobic conditions, indicating increased activity of PFL.
overproducing of the enzyme in Escherichia coli 234M1 transformed with expression vector p153E1
Escherichia coli SP 264 contains plasmid p29with pfl gene, identification of pfl gene product as a 80kDa polypeptide
-
gene pfl from strain JM109, DNA and amino acid sequence determination and analysis, expression of His-tagged wild-type and mutant enzymes in strain BL21(DE3)
-
overexpression of the His6-tagged enzyme as single enzyme or as AdhE-Pfl in strain BL21(DE3)
-
structural gene pfl cloned and sequenced, homologous expression and overproduction in Escherichia coli K12
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
coexpression of either of the electron donors reduced ferredoxin or reduced flavodoxin has a positive effect on growth under aerobic conditions, indicating increased activity of PFL. with a higher final biomass concentration and a significant increase in transcription of formate dehydrogenases
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 butyricum DSM 552, Clostridium kluyveri, Clostridium pasteurianum, Clostridium pasteurianum (Q46266), Clostridium pasteurianum DSM 525, Clostridium sp., Enterococcus faecalis, Escherichia coli, no activity in Clostridium pasteurianum, Streptococcus mutans, Streptococcus salivarius, Streptococcus sanguinis, Streptococcus sanguinis DSM 20066
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
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
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
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
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
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
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
-
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
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
-
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
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
-
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
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
-
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
-
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)
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
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
Escherichia coli, Escherichia coli (P09373), Haemophilus influenzae, Pasteurella multocida, Salmonella enterica subsp. enterica serovar Typhimurium, Tequatrovirus T4, Vibrio cholerae serotype O1, Yersinia pestis
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
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)
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)
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
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.
58
338-344
2002
Escherichia coli, Lactococcus lactis
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.
186
7593-7600
2004
Escherichia coli
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.
466
45-48
2000
Escherichia coli
De Lucas, M.; Fernandes, P.A.; Eriksson, L.A.; Ramos, M.J.
Pyruvate formate lyase: a new perspective
J. Phys. Chem. B
107
5751-5757
2003
Escherichia coli
-
Nnyepi, M.R.; Peng, Y.; Broderick, J.B.
Inactivation of E. coli pyruvate formate-lyase: role of AdhE and small molecules
Arch. Biochem. Biophys.
459
1-9
2007
Escherichia coli
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
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.
97
138-143
2007
Escherichia coli
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.
127
6902-6909
2005
Escherichia coli
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.
29
2425-2433
2008
Escherichia coli (P09373)
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 (P09373)
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
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
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
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)
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
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)
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)
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