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Enzyme Nomenclature
Information on EC 2.3.1.54 - formate C-acetyltransferase
Word Map on EC 2.3.1.54
- 2.3.1.54
- lactate
- ethanol
-
glycyl
-
ribonucleotide
- phosphotransacetylase
-
mixed-acid
-
microaerobic
-
anaerobiosis
-
homolactic
- acetoin
-
pyruvate:ferredoxin
-
glucose-limited
-
activase
-
oxygen-sensitive
-
flavodoxins
-
5\'-deoxyadenosyl
-
dual-phase
-
knappe
- benzylsuccinate
-
2,3-aminomutase
-
embden-meyerhof-parnas
- 5'-deoxyadenosine
- hypophosphite
- nutrition
- biotechnology
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.3.1.54
-
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RECOMMENDED NAME
GeneOntology No.
formate C-acetyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + formate = CoA + pyruvate
-
-
-
-
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
part of a bacterial-type mixed-acid fermentation in combination with alcohol dehydrogenase E
-
acetyl-CoA + formate = CoA + pyruvate
the reaction mechanism proceeds via generation of a catalytically essential glycyl radical at Gly734
-
acetyl-CoA + formate = CoA + pyruvate
catalytic mechanism involving residues Gly734, Cys418 and Cys419, transition state, modeling, overview
-
acetyl-CoA + formate = CoA + pyruvate
active site structure includes an active site tunnel, substrate binding at Asp447 at the protein surface
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:formate C-acetyltransferase
-
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CAS REGISTRY NUMBER
COMMENTARY
9068-08-0
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
wild-type and mutant strains, anaerobic growth conditions
-
-
no activity in Clostridium pasteurianum
slightly aerobic and anaerobic growth, and intraperitoneal infection or nasal infection of female MFI mice
-
-
DSM525, nucleotide sequence accession number, GenBank and EMBL
SwissProt
-
14931, 14932, 487218, 487219, 487222, 487225, 487226, 487227, 487228, 487230, 487231, 487233, 487235, 487236, 487237, 487240, 659056, 661722, 662704, 674168
-
-
PFL wild-type, structure factor amplitude and model coordinate, Protein Data Bank accession code
SwissProt
wild-type and arcA-/- strains, MG1655, MG1655, MG1655, and MG1655, gene pfl
-
-
formerly designated Streptococcus cremoris; formerly designated Streptococcus lactis
-
-
wild-type JB1 pfl, GenBank nucleotide sequence accession number
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
-
anaerobic fermentation pathway yielding 3 ATP per glucose, pyruvate channeling to fermentation product, lactate dehydrogenase and pyruvate dehydrogenase are alternative pyruvate channeling enzymes during fermentation
metabolism
-
anaerobic glucose metabolism, direct link between fermentative metabolism and virulence in infected mice
metabolism
the enzyme takes part in the metabolic pathway of pyruvate to ethanol in Thermoanaerobacterium saccharolyticum
metabolism
-
NADH generated from anaerobic glycerol metabolism in the absence of fumarate is oxidized through the pyruvate formate-lyase-ethanol fermentation pathway. Thus, the enzyme is essential to avoid the accumulation of excess NADH during fumarate-independent anaerobic glycerol metabolism
metabolism
-
NADH generated from anaerobic glycerol metabolism in the absence of fumarate is oxidized through the pyruvate formate-lyase-ethanol fermentation pathway. Thus, the enzyme is essential to avoid the accumulation of excess NADH during fumarate-independent anaerobic glycerol metabolism
-
metabolism
-
the enzyme takes part in the metabolic pathway of pyruvate to ethanol in Thermoanaerobacterium saccharolyticum
-
physiological function
-
enzyme deletion mutant displays pleiotropic effects. In the mutant, no formate is produced, glucose consumption is delayed, and ethanol production is decreased, whereas acetate and lactate production are unaffected. All metabolic alterations can be restored by addition of formate or complementation of the mutant. In compensation reactions, serine and threonine are consumed better by the mutant than by the wild-type. The mutant displays reduced production of formylated peptides compared to the parental strain. Arginine consumption and arc operon transcription are increased in the mutant. Enzyme plays a significant role in the anaerobic layer of a biofilm
physiological function
the physiological role of pyruvate formate-lyase is supplying C1 units for biosyntheses
physiological function
anaerobic alkane degradation in Archaeoglobus fulgidus may involve the gene pflD in alkane activation through addition to fumarate
physiological function
-
enzyme pyruvate formate-lyase is responsible for intracellular formate generation in enterobacteria and other microbes
physiological function
-
the physiological role of pyruvate formate-lyase is supplying C1 units for biosyntheses
-
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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
acetyl-CoA + formate
CoA + pyruvate
-
-
-
?
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
-
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
-
anaerobic growth under nitrogen, 37°C, pH 7.0, extract enzyme reactions measured at room temperature
-
-
?
CoA + pyruvate
acetyl-CoA + formate
-
metabolic regulation and networking, overview
-
-
?
CoA + pyruvate
acetyl-CoA + formate
Q5LYC1
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
Q5LYC1
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
-
required for synthesis of C1 units in anabolism
-
-
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
-
required for synthesis of C1 units in anabolism
-
-
-
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
required for synthesis of C1 units in anabolism
-
-
-
pyruvate + CoA
acetyl-CoA + formate
-
required for synthesis of C1 units in anabolism
-
-
-
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
-
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
-
-
-
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 + 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
-
central reaction in the anaerobic metabolism
-
-
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
-
catabolic function, leading to production of ATP
-
-
-
pyruvate + CoA
acetyl-CoA + formate
-
catabolic function, leading to production of ATP
-
-
ir
pyruvate + CoA
formate + acetyl-CoA
-
mixed-acid fermentation, necessary for growth in xylose minimal medium under anaerobic conditions
-
-
r
pyruvate + dithiothreitol
S-acetyl-dithiothreitol + formate
-
-
-
?
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
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
Q5LYC1
analysis of the cytosolic proteome involving the enzyme, proteome profile
-
-
-
additional information
?
-
-
analysis of the cytosolic proteome involving the enzyme, proteome profile
-
-
-
additional information
?
-
Q5LYC1
analysis of the cytosolic proteome involving the enzyme, proteome profile
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
acetyl-CoA + formate
CoA + pyruvate
I3VT07
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
Q1RS83
step in the mitochondrial pathway, overview
-
-
?
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
-
metabolic regulation and networking, overview
-
-
?
CoA + pyruvate
acetyl-CoA + formate
Q5LYC1
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
Q5LYC1
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
-
required for synthesis of C1 units in anabolism
-
-
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
-
required for synthesis of C1 units in anabolism
-
-
-
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
Q46266
required for synthesis of C1 units in anabolism
-
-
-
pyruvate + CoA
acetyl-CoA + formate
-
required for synthesis of C1 units in anabolism
-
-
-
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
-
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
P09373
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 + 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
-
central reaction in the anaerobic metabolism
-
-
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
-
catabolic function, leading to production of ATP
-
-
-
pyruvate + CoA
acetyl-CoA + formate
-
catabolic function, leading to production of ATP
-
-
ir
pyruvate + CoA
formate + acetyl-CoA
-
mixed-acid fermentation, necessary for growth in xylose minimal medium under anaerobic conditions
-
-
r
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
?
-
-
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
?
-
Q5LYC1
analysis of the cytosolic proteome involving the enzyme, proteome profile
-
-
-
additional information
?
-
-
analysis of the cytosolic proteome involving the enzyme, proteome profile
-
-
-
additional information
?
-
Q5LYC1
analysis of the cytosolic proteome involving the enzyme, proteome profile
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITORS
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
-
ATP
-
regulates pyruvate cleavage to acetyl-CoA and formate, 10 mM reduces the reactin velocity by 95%
ATP
-
regulates pyruvate cleavage to acetyl-CoA and formate, 10 mM reduces the reactin velocity by 95%
ATP
-
regulates pyruvate cleavage to acetyl-CoA and formate, 10 mM reduces the reactin velocity by 95%
CoA
-
inhibits exchange reaction between pyruvate and formate, inhibits formate formation from pyruvate above 0.075 mM
CoA
-
inhibits exchange reaction between pyruvate and formate, inhibits formate formation from pyruvate above 0.075 mM
CoA
-
inhibits exchange reaction between pyruvate and formate, inhibits formate formation from pyruvate above 0.075 mM
DEAE-cellulose
-
treated extracts do not catalyze formate formation from pyruvate
-
DEAE-cellulose
-
treated extracts do not catalyze formate formation from pyruvate
-
DEAE-cellulose
-
treated extracts do not catalyze formate formation from pyruvate
-
methacrylate
-
suicide inhibition mechanism, possibly involving also Arg176 and Arg435, binds to Cys419, modeling, overview
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
-
more effective for activation than NADPH, 0.02 mM NADPH activates over 80% inactive enzyme in cell-free extracts
Y06I
-
autonomous glycyl radical cofactor, reconstituting the catalytic center of oxygen-fragmented enzyme
-
additional information
-
conversion into the active form is carried out by an activating system containing a flavodoxin system and an activating enzyme (pyruvate format lyase-activase, EC 1.97.1.4)
-
Ferredoxin
-
reactivation of inactive enzyme requires reduced ferredoxin, Fe2+-dithiol or Co2+-mercaptoethanol complexes can substitute for ferredoxin
-
Ferredoxin
-
reactivation of inactive enzyme requires reduced ferredoxin, Fe2+-dithiol or Co2+-mercaptoethanol complexes can substitute for ferredoxin
-
Ferredoxin
-
reactivation of inactive enzyme requires reduced ferredoxin, Fe2+-dithiol or Co2+-mercaptoethanol complexes can substitute for ferredoxin
-
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
-
S-adenosylmethionine
-
obligatory component of the activation reaction
S-adenosylmethionine
-
obligatory component of the activation reaction
YfiD
; autonomous glycyl radical cofactor, reconstituting the catalytic center of oxygen-fragmented enzyme
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
steady-state kinetics of wild-type and mutant enzymes
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
ethanol-producing fermentative metabolism in Chlamydomonas reinhardtii proposed to be initiated by pyruvate formate-lyase, heterologous expression of Chlamydomonas Pfl1 protein in pyruvate formate-lyase-deficient strain of Escherichia coli, enzmye activity under anaerobic conditions regained, Pfl1 fermentation pathway of Chlamydomonas reinhardtii under physiological condition of sulfur depletion analyzed, formate accumulation measured
additional information
ethanol-producing fermentative metabolism in Chlamydomonas reinhardtii proposed to be initiated by pyruvate formate-lyase, heterologous expression of Chlamydomonas Pfl1 protein in pyruvate formate-lyase-deficient strain of Escherichia coli, enzmye activity under anaerobic conditions regained, Pfl1 fermentation pathway of Chlamydomonas reinhardtii under physiological condition of sulfur depletion analyzed, formate accumulation measured
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 7.5
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8.3
-
40% of activity maximum at pH 6.5, between pH 7.0-8.3 80% of maximum activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
formate accumulation in the medium of anaerobically adapted Chlamydomonas reinhardtii CC-277 cells measured
formate accumulation inside anaerobically adapted Chlamydomonas reinhardtii CC-277 cells measured
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microaerobic cultures, glucose-limited chemostat cultures, different strains, growth rates, overview
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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
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80000 - 85000
83000
85000
87000
95000
-
4 * 95000, structure analysis, crystal packing, solution X-ray scattering, and ultracentrifugation
83000
-
1 * 87000 + 1 * 83000, TOF-MS flight mass spectrometry, SDS-PAGE
83000
1 * 87000 + 1 * 83000, TOF-MS flight mass spectrometry, SDS-PAGE
87000
-
1 * 87000 + 1 * 83000, TOF-MS flight mass spectrometry, SDS-PAGE
87000
1 * 87000 + 1 * 83000, TOF-MS flight mass spectrometry, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
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4 * 95000, structure analysis, crystal packing, solution X-ray scattering, and ultracentrifugation
additional information
dimer
-
2 * 85000, homodimer, SDS-PAGE
dimer
-
; 2 * 70000; 2 * 85000, homodimer, SDS-PAGE; 2 * 85000, homodimer, SDS-PAGE; 2 * 85500, homodimer, SDS-PAGE
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dimer
-
1 * 87000 + 1 * 83000, TOF-MS flight mass spectrometry, SDS-PAGE; 2 * 80000-90000, SDS-PAGE
dimer
1 * 87000 + 1 * 83000, TOF-MS flight mass spectrometry, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified enzyme, sitting drop vapour diffusion method, mixing 0.001 ml of 20 mg/ml protein solution with 0.001 ml precipitant solution containing 16% w/v PEG 8000, 8% v/v isopropanol, 80 mM Hepes, pH 7.5, 160 mM ammonium sulfate and 1 mM DTT, plate-like crystals, X-ray diffraction structure determination and analysis at 2.9 A resolution
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three-dimensional modeling of the corresponding protein and molecular dynamic simulations, predict an alkylsuccinate synthase activity. The four stereoisomers of (1-methyl-pentadecyl)succinate formed by addition of the sub-terminal carbon atom (C-2) of hexadecane to fumarate are able to exit the protein tunnel
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
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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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PFL2 appears to be stabilized by several factors including an increased number of ion pairs, differences in buried charges, a truncated N terminus, anchoring of loops and N terminus via salt-bridges,changes in the oligomeric interface and perhaps also the higher oligomerization state of the protein
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stable for 2 h at 35°C in untreated cell-free extracts under strictly anaerobic conditions. In dialyzed cell-free extracts, activity decreases gradually.
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virtually stable at 0°C and pH 8.0 if kept in media which display a redoxpotential of 0.2 V or below
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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
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487225, 487226, 487236
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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
-
4°C, 50 mM potassium phosphate buffer, containing 1 mM dithiothreitol, storage of the purified enzyme in an anaerobic glove box for 2 weeks reduces activity by 50%
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
centrifugation, washing in 50 mM potassium phosphate buffer, pH 7.5, resuspension, French press disruption, centrifugation of crude extract and of resulting supernatant
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gel filtration, Western Blot, heterologously expressed protein
native enzyme at pH 6.4, by anion exchange and hydrophobic interaction chromatography, and gel filtration, to homogeneity
-
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
-
recombinant enzyme
recombinant His-tagged wild-type and mutant enzymes from strain BL21(DE3) by nickel affinity chromatography to homogeneity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Escherichia coli SP 264 contains plasmid p29with pfl gene, identification of pfl gene product as a 80kDa polypeptide
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expressed in Escherichia coli BL21(DE3), pET9a expression vector, transformation into pyruvate formate-lyase-deficient Escherichia coli strain BL21, capacity for formate excretion shown by in vitro tests
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)
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gene pfl, DNA and amino acid sequence determination and analysis, detailed phylogenetic analysis, overview
gene pfl, DNA and amino acid sequence determination and analysis, sequence comparison
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gene pflB, overexpression of the enzyme from plasmid 29 in the soluble fraction of Escherichia coli strain MC4100
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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.
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overexpression of the His6-tagged enzyme as single enzyme or as AdhE-Pfl in strain BL21(DE3)
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overproducing of the enzyme in Escherichia coli 234M1 transformed with expression vector p153E1
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pfl gene expressed under control of different constitutive promoters, PFL-deficient strain CRM40 complemented
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structural gene pfl cloned and sequenced, homologous expression and overproduction in Escherichia coli K12
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
9fold increase in SPD0420 mutants in galactose compared to glucose-grown bacteria in anaerobic conditions, in aerobiosis, 2.4fold upregulation of SpD0420 mutant, 3.5fold in SPD1774 mutant in galactose compared to glucose-grown bacteria
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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
-
expression of pyruvate formate-lyase is upregulated during anaerobic culture with glycerol
in all pyruvate ferredoxin oxidoreductase enzyme, gene pfor deletion strains, the expression levels of pyruvate formate-lyase genes are increased about sixfold compared with the parent strain. The strains show different growth dependent on the medium used
pflD gene expression is upregulated during the growth of Archaeoglobus fulgidus on an n-alkane (C16) compared with growth on a fatty acid
expression of pyruvate formate-lyase is upregulated during anaerobic culture with glycerol
-
expression of pyruvate formate-lyase is upregulated during anaerobic culture with glycerol
-
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in all pyruvate ferredoxin oxidoreductase enzyme, gene pfor deletion strains, the expression levels of pyruvate formate-lyase genes are increased about sixfold compared with the parent strain. The strains show different growth dependent on the medium used
in all pyruvate ferredoxin oxidoreductase enzyme, gene pfor deletion strains, the expression levels of pyruvate formate-lyase genes are increased about sixfold compared with the parent strain. The strains show different growth dependent on the medium used
-
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A273C
-
site-directed mutagenesis, the mutant is less thermostable than the wild-type enzyme
E336C
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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
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
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E400I
-
site-directed mutagenesis, the mutant is more thermostable than the wild-type enzyme, Tm is increased 2.2fold, half-life 2.21fold
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additional information
additional information
-
construction of a pflB gene disruptant of strain W11 that barely utilizes glycerol under anaerobic conditions, but the growth of the DELTApfl mutant strain cultured with either glucose or dihydroxyacetone under anaerobic conditions is the same as that of wild-type strain W11
additional information
-
construction of a pflB gene disruptant of strain W11 that barely utilizes glycerol under anaerobic conditions, but the growth of the DELTApfl mutant strain cultured with either glucose or dihydroxyacetone under anaerobic conditions is the same as that of wild-type strain W11
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additional information
-
deletion of both pflA and pflB (strain RM220) partially restores the ability of the strain to respond to exogenous formate
additional information
-
mutant strain CL3 with deletions in pflB, adhE, and frdA genes producing D-lactate from glucose, 44% slower growth under anaerobic conditions, 2.8fold higher glycolytic flux, 95% lactate yield, 22% lower ATP/ADP ratio
additional information
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mutant strain YK167 lacking pyruvate formate-lyase shows almost 50% increase in glucose consumption and flux with higher flux to lactate and lower ATP-yield, double mutant for pyruvate formate-lyase and lactate dehydrogenase (strain SE2382) shows 50% lower glucose flux and ATP yield than strain YK167 and results in reduced cell mass growth
additional information
-
no formate production and decrease of unsaturation index in downstream (in absence of acetate) fatty acid production in mutants SPD0420M (enzyme mutant) and SPD1774M (activating enzyme mutant), restored by complementation, increased survival and lower disease sign score of mice infected with mutant strains, wild-type survival rate in complemented mutants, lower nasopharynx numbers and lower survival in lungs, intravenous infection with similar growth of mutant and wild-type. All mutant and wild-type strains grow better under aerobic than anaerobic conditions with glucose as sole carbon source, no difference in growth rate and yields between mutants and wild-type, with galactose (generally lower growth rate than with glucose) as carbon source all but strain SPD1774M grow better under aerobic conditions, strain SPD1774M better under anaerobic conditions, strain SPD0420M has lower growth rate than wild-type under anaerobiosis, the complemented strain SPD0420Comp grows better than SPD0420M in anaerobiosis. Mutants SPD035M and SPD0229M do not affect pyruvate formate lyase dependent product formation.
additional information
construction of the pfl deletion resulting in two different strains LL1164 and LL1170 with two different phenotypes, high lactate and low lactate, respectively. Of eight colonies picked, two have the LL1164 phenotype and six have the LL1170 phenotype. Strain LL1170 consumes more cellobiose, produces more acetate and ethanol and less lactate than strain LL1164. A pfor/pfl double deletion strain LL1178 consumes about 70% of the 5 g/L cellobiose initially present, which is about the same as its parent strain LL1141. It requires sodium acetate for growth, even in the presence of yeast extract. Lactate is the main product of fermentation
additional information
-
construction of the pfl deletion resulting in two different strains LL1164 and LL1170 with two different phenotypes, high lactate and low lactate, respectively. Of eight colonies picked, two have the LL1164 phenotype and six have the LL1170 phenotype. Strain LL1170 consumes more cellobiose, produces more acetate and ethanol and less lactate than strain LL1164. A pfor/pfl double deletion strain LL1178 consumes about 70% of the 5 g/L cellobiose initially present, which is about the same as its parent strain LL1141. It requires sodium acetate for growth, even in the presence of yeast extract. Lactate is the main product of fermentation
additional information
-
construction of the pfl deletion resulting in two different strains LL1164 and LL1170 with two different phenotypes, high lactate and low lactate, respectively. Of eight colonies picked, two have the LL1164 phenotype and six have the LL1170 phenotype. Strain LL1170 consumes more cellobiose, produces more acetate and ethanol and less lactate than strain LL1164. A pfor/pfl double deletion strain LL1178 consumes about 70% of the 5 g/L cellobiose initially present, which is about the same as its parent strain LL1141. It requires sodium acetate for growth, even in the presence of yeast extract. Lactate is the main product of fermentation
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
D-lactate production for the use in biopolymer production as biodegradable alternative for oil-derived plastics
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LINKS TO OTHER DATABASES (specific for EC-Number 2.3.1.54)
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