Information on EC 2.3.1.54 - formate C-acetyltransferase

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The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria, dsDNA viruses, no RNA stage

EC NUMBER
COMMENTARY
2.3.1.54
-
RECOMMENDED NAME
GeneOntology No.
formate C-acetyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
acetyl-CoA + formate = CoA + pyruvate
show the reaction diagram
-
-
-
-
acetyl-CoA + formate = CoA + pyruvate
show the reaction diagram
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
show the reaction diagram
part of a bacterial-type mixed-acid fermentation in combination with alcohol dehydrogenase E
-
acetyl-CoA + formate = CoA + pyruvate
show the reaction diagram
the reaction mechanism proceeds via generation of a catalytically essential glycyl radical at Gly734
-
acetyl-CoA + formate = CoA + pyruvate
show the reaction diagram
reaction via glycyl radical
-
acetyl-CoA + formate = CoA + pyruvate
show the reaction diagram
catalytic mechanism involving residues Gly734, Cys418 and Cys419, transition state, modeling, overview
-
acetyl-CoA + formate = CoA + pyruvate
show the reaction diagram
active site structure includes an active site tunnel, substrate binding at Asp447 at the protein surface
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Butanoate metabolism
-
Metabolic pathways
-
mixed acid fermentation
-
Propanoate metabolism
-
pyruvate fermentation to acetate IV
-
pyruvate fermentation to ethanol I
-
Pyruvate metabolism
-
reductive monocarboxylic acid cycle
-
respiration (anaerobic)
-
superpathway of fermentation (Chlamydomonas reinhardtii)
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:formate C-acetyltransferase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
formate acetyltransferase
-
-
-
-
PFL
Clostridium thermocellum 27405.
-
-
-
PFL
P09373
-
PFL
Escherichia coli JM109
-
-
-
PFL
Escherichia coli K12
-
;
-
PFL
Streptococcus thermophilus LMG18311
Q5LYC1
-
-
phosphotransferase system enzyme I
-
-
phosphotransferase system enzyme I
Escherichia coli K12
-
-
-
pyruvate formate lyase
-
-
pyruvate formate lyase
-
-
pyruvate formate lyase
-
mutant strain CL3 with deletions in pflB, adhE, and frdA genes affecting D-lactate production
pyruvate formate lyase
Q6RFH7
-
pyruvate formate lyase
-
-
pyruvate formate-lyase
-
-
-
-
pyruvate formate-lyase
P37836
-
pyruvate formate-lyase
Q1RS83
-
pyruvate formate-lyase
-
-
pyruvate formate-lyase
Clostridium thermocellum 27405.
-
-
-
pyruvate formate-lyase
-
-
pyruvate formate-lyase
P09373
-
pyruvate formate-lyase
Escherichia coli JM109
-
-
-
pyruvate formate-lyase
-
-
pyruvate formate-lyase
Q5LYC1
-
pyruvate formate-lyase
Streptococcus thermophilus LMG18311
Q5LYC1
-
-
pyruvate-formate lyase
-
-
pyruvate:formate lyase
-
-
pyruvic formate-lyase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9068-08-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
a hyperthermophile, gene pfl2
-
-
Manually annotated by BRENDA team
strain CC-125 and cell wall-less strain CC-277
SwissProt
Manually annotated by BRENDA team
Clostridium butylicum
ATCC 14823
-
-
Manually annotated by BRENDA team
Clostridium butyricum DSM552
DSM552
-
-
Manually annotated by BRENDA team
DSM525, nucleotide sequence accession number, GenBank and EMBL
SwissProt
Manually annotated by BRENDA team
Clostridium pasteurianum DSM525
DSM525
-
-
Manually annotated by BRENDA team
gene pfl, strain 27405
-
-
Manually annotated by BRENDA team
previously Streptococcus faecalis
-
-
Manually annotated by BRENDA team
ATCC 10798; K12
-
-
Manually annotated by BRENDA team
gene pfl
-
-
Manually annotated by BRENDA team
PFL wild-type, structure factor amplitude and model coordinate, Protein Data Bank accession code
SwissProt
Manually annotated by BRENDA team
PFL, SwissProt accession number
SwissProt
Manually annotated by BRENDA team
strain JM109
-
-
Manually annotated by BRENDA team
wild-type and arcA-/- strains, MG1655, MG1655, MG1655, and MG1655, gene pfl
-
-
Manually annotated by BRENDA team
Escherichia coli JM109
strain JM109
-
-
Manually annotated by BRENDA team
Escherichia coli K12
K12
-
-
Manually annotated by BRENDA team
wild-type and mutant strains, anaerobic growth conditions
-
-
Manually annotated by BRENDA team
formerly designated Streptococcus cremoris; formerly designated Streptococcus lactis
-
-
Manually annotated by BRENDA team
formerly designated Streptococcus lactis
-
-
Manually annotated by BRENDA team
subsp. cremoris, MG1363
-
-
Manually annotated by BRENDA team
no activity in Clostridium pasteurianum
-
-
-
Manually annotated by BRENDA team
no activity in Clostridium pasteurianum
ATCC 6013
-
-
Manually annotated by BRENDA team
strain MR-1, gene pflB
-
-
Manually annotated by BRENDA team
wild-type JB1 pfl, GenBank nucleotide sequence accession number
SwissProt
Manually annotated by BRENDA team
Streptococcus mutans JC2
JC2
-
-
Manually annotated by BRENDA team
slightly aerobic and anaerobic growth, and intraperitoneal infection or nasal infection of female MFI mice
-
-
Manually annotated by BRENDA team
Streptococcus sanguinis DSM20066
DSM20066
-
-
Manually annotated by BRENDA team
strain LMG18311, gene pfl
SwissProt
Manually annotated by BRENDA team
Streptococcus thermophilus LMG18311
strain LMG18311, gene pfl
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxobutyrate + CoA
acetyl-CoA + acetate
show the reaction diagram
-
-
-
-
r
acetyl-CoA + formate
pyruvate + CoA
show the reaction diagram
-
-
-
-
r
acetyl-CoA + formate
pyruvate + CoA
show the reaction diagram
P09973
-
-
-
r
acetyl-CoA + formate
pyruvate + CoA
show the reaction diagram
P09373
-
-
-
r
acetyl-CoA + formate
pyruvate + CoA
show the reaction diagram
-
-
-
-
r
acetyl-CoA + formate
pyruvate + CoA
show the reaction diagram
-
-
-
-
r
acetyl-CoA + formate
pyruvate + CoA
show the reaction diagram
Escherichia coli K12
-
-
-
-
r
CoA + pyruvate
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
show the reaction diagram
-, Q1RS83
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
show the reaction diagram
Q5LYC1, -
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
show the reaction diagram
-, P37836
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
show the reaction diagram
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
show the reaction diagram
-
metabolic regulation and networking, overview
-
-
?
CoA + pyruvate
acetyl-CoA + formate
show the reaction diagram
-, Q1RS83
step in the mitochondrial pathway, overview
-
-
?
CoA + pyruvate
acetyl-CoA + formate
show the reaction diagram
-
the reaction involves Cys418 and Cys419
-
-
?
CoA + pyruvate
acetyl-CoA + formate
show the reaction diagram
-, P37836
anaerobic metabolism and potential ethanol-producing pathways in Chlamydomonas reinhardtii analyzed
-
-
?
CoA + pyruvate
acetyl-CoA + formate
show the reaction diagram
-
mechanism to truncate an arginine-bound carboxylate motif, substrate mechanism of pyruvate formate-lyase used as a case study
-
-
?
CoA + pyruvate
acetyl-CoA + formate
show the reaction diagram
-
anaerobic growth under nitrogen, 37C, pH 7.0, extract enzyme reactions measured at room temperature
-
-
?
CoA + pyruvate
acetyl-CoA + formate
show the reaction diagram
Streptococcus thermophilus LMG18311
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
show the reaction diagram
Escherichia coli JM109
-
-
-
-
?
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
P09373
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
P09373
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
P09973
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
P09373
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
O66391, -
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
O66391, -
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
ir
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-, Q46266
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
-, ?
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
Clostridium butylicum
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
-, r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
-, ?
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-, Q46266
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
reverse reaction with only 0.1% velocity of the forward reaction
-
-
ir, r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
no report on the reverse reaction
-
-
ir, r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
central reaction in the anaerobic metabolism
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
key enzyme of the glucose fermentation route in anaerobically growing cells
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
P09373
key enzyme of the glucose fermentation route in anaerobically growing cells
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
key enzyme of the glucose fermentation route in anaerobically growing cells
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
key role in the metabolism
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-, Q46266
required for synthesis of C1 units in anabolism
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
required for synthesis of C1 units in anabolism
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
required for synthesis of C1 units in anabolism
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
required for synthesis of C1 units in anabolism
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
Clostridium kluyveri, Clostridium butylicum
-
required for synthesis of C1 units in anabolism
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
physiological function is both anabolic and catabolic
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
acetyl-CoA for ATP synthesis in catabolism
-
-
ir, r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
catabolic function, leading to production of ATP
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
catabolic function, leading to production of ATP
-
-
ir, r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
catabolic function, leading to production of ATP
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
catabolic function, leading to production of ATP
-
-
ir, r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
catabolic function, leading to production of ATP
-
-
ir
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
catabolic function, leading to production of ATP
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
main enzyme competing for pyruvate under anaerobic conditions
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
Clostridium butyricum DSM552
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
Clostridium butyricum DSM552
-
required for synthesis of C1 units in anabolism
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
-, r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
-, r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
Streptococcus mutans JC2
-
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
Clostridium pasteurianum DSM525
-
-, required for synthesis of C1 units in anabolism
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
Escherichia coli K12
-
-, key enzyme of the glucose fermentation route in anaerobically growing cells
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
Escherichia coli K12
-
-, key enzyme of the glucose fermentation route in anaerobically growing cells
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
Escherichia coli K12
-
-, key role in the metabolism
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
Escherichia coli K12
-
-, central reaction in the anaerobic metabolism
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
Escherichia coli K12
-
-
-
-
-, r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
Streptococcus sanguinis DSM20066
-
-
-
-
-, r
pyruvate + CoA
formate + acetyl-CoA
show the reaction diagram
-
-
-
-
r
pyruvate + CoA
formate + acetyl-CoA
show the reaction diagram
-
mixed-acid fermentation, necessary for growth in xylose minimal medium under anaerobic conditions
-
-
r
pyruvate + dephospho-CoA
dephospho-acetyl-CoA + formate
show the reaction diagram
-
-
-
-
r
pyruvate + dithiothreitol
S-acetyl-dithiothreitol + formate
show the reaction diagram
Escherichia coli, Escherichia coli K12
-
-
-
?
pyruvate + formate
pyruvate + formate
show the reaction diagram
-
carboxyl group exchange reaction
-
r
pyruvate + formate
pyruvate + formate
show the reaction diagram
-
carboxyl group exchange reaction
-
r
pyruvate + formate
pyruvate + formate
show the reaction diagram
-
carboxyl group exchange reaction
-
r
pyruvate + formate
pyruvate + formate
show the reaction diagram
-
carboxyl group exchange reaction
-
r
pyruvate + formate
pyruvate + formate
show the reaction diagram
-
carboxyl group exchange reaction
-
r
pyruvate + formate
pyruvate + formate
show the reaction diagram
Escherichia coli K12
-
carboxyl group exchange reaction
-
r
pyruvate + phosphate
acetylphosphate + formate
show the reaction diagram
-
-
-
ir
CoA + pyruvate
acetyl-CoA + formate
show the reaction diagram
Clostridium thermocellum 27405.
-
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
phosphate cannot substitute for CoA
-
-
-
additional information
?
-
-
not essential for nitrate respiration
-
-
-
additional information
?
-
Q5LYC1, -
analysis of the cytosolic proteome involving the enzyme, proteome profile
-
-
-
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
?
-
-
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
?
-
-
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
?
-
Streptococcus thermophilus LMG18311
Q5LYC1
analysis of the cytosolic proteome involving the enzyme, proteome profile
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + formate
pyruvate + CoA
show the reaction diagram
Escherichia coli, Escherichia coli K12
-
-
-
-
r
CoA + pyruvate
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
show the reaction diagram
-, P37836
-
-
-
?
CoA + pyruvate
acetyl-CoA + formate
show the reaction diagram
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
show the reaction diagram
-
metabolic regulation and networking, overview
-
-
?
CoA + pyruvate
acetyl-CoA + formate
show the reaction diagram
-, Q1RS83
step in the mitochondrial pathway, overview
-
-
?
CoA + pyruvate
acetyl-CoA + formate
show the reaction diagram
-
anaerobic growth under nitrogen, 37C, pH 7.0, extract enzyme reactions measured at room temperature
-
-
?
CoA + pyruvate
acetyl-CoA + formate
show the reaction diagram
Streptococcus thermophilus LMG18311
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
show the reaction diagram
Escherichia coli JM109
-
-
-
-
?
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
P09373
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
P09973
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
O66391, -
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-, Q46266
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
central reaction in the anaerobic metabolism
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
key enzyme of the glucose fermentation route in anaerobically growing cells
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
P09373
key enzyme of the glucose fermentation route in anaerobically growing cells
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
key enzyme of the glucose fermentation route in anaerobically growing cells
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
key role in the metabolism
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-, Q46266
required for synthesis of C1 units in anabolism
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
required for synthesis of C1 units in anabolism
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
required for synthesis of C1 units in anabolism
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
required for synthesis of C1 units in anabolism
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
Clostridium kluyveri, Clostridium butylicum
-
required for synthesis of C1 units in anabolism
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
physiological function is both anabolic and catabolic
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
acetyl-CoA for ATP synthesis in catabolism
-
-
ir, r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
catabolic function, leading to production of ATP
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
catabolic function, leading to production of ATP
-
-
ir, r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
catabolic function, leading to production of ATP
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
catabolic function, leading to production of ATP
-
-
ir, r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
catabolic function, leading to production of ATP
-
-
ir
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
catabolic function, leading to production of ATP
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
main enzyme competing for pyruvate under anaerobic conditions
-
-
r
pyruvate + CoA
formate + acetyl-CoA
show the reaction diagram
-
-
-
-
r
pyruvate + CoA
formate + acetyl-CoA
show the reaction diagram
-
mixed-acid fermentation, necessary for growth in xylose minimal medium under anaerobic conditions
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
Clostridium butyricum DSM552
-
required for synthesis of C1 units in anabolism
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
-
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
Streptococcus mutans JC2
-
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
Clostridium pasteurianum DSM525
-
required for synthesis of C1 units in anabolism
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
Escherichia coli K12
-
key enzyme of the glucose fermentation route in anaerobically growing cells
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
Escherichia coli K12
-
key enzyme of the glucose fermentation route in anaerobically growing cells
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
Escherichia coli K12
-
key role in the metabolism
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
Escherichia coli K12
-
central reaction in the anaerobic metabolism
-
-
r
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
Escherichia coli K12
-
-
-
-
-
pyruvate + CoA
acetyl-CoA + formate
show the reaction diagram
Streptococcus sanguinis DSM20066
-
-
-
-
-
CoA + pyruvate
acetyl-CoA + formate
show the reaction diagram
Clostridium thermocellum 27405.
-
-
-
-
?
additional information
?
-
Q5LYC1, -
analysis of the cytosolic proteome involving the enzyme, proteome profile
-
-
-
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
?
-
-
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
?
-
Streptococcus thermophilus LMG18311
Q5LYC1
analysis of the cytosolic proteome involving the enzyme, proteome profile
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Mg2+
-
stimulates pyruvate cleavage about 2fold
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
rapid, reversible inactivation, deactivation is a non-destructive transfer of an H atom equivalent to quench the glycyl radical
Acetylphosphinate
-
mechanism-based inactivator
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
D-Glyceraldehyde-3-phosphate
-
-
D-Glyceraldehyde-3-phosphate
-
-
D-Glyceraldehyde-3-phosphate
-
-
DEAE-cellulose
-
treated extracts do not catalyze formate formation from pyruvate
-
dihydroxyacetone phosphate
-
-
dihydroxyacetone phosphate
-
-
dihydroxyacetone phosphate
-
-
DTT
-
reversible inactivation, deactivation is a non-destructive transfer of an H atom equivalent to quench the glycyl radical
formate
-
product inhibition
HPO42-
-
-
Hypophosphite
-
strongly inhibits formate formation from pyruvate
Hypophosphite
-, P37836
formate formation from pyruvate inhibited
iodoacetate
-
-
methacrylate
-
substrate-analogue suicide inhibitor
-
Oxamate
-
isosteric, chemically inert pyruvate analogue
S-adenosyl-L-homocysteine
-
-
S-adenosyl-L-homocysteine
-
-
SO42-
-
-
methacrylate
-
suicide inhibition mechanism, possibly involving also Arg176 and Arg435, binds to Cys419, modeling, overview
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Ferredoxin
-
reactivation of inactive enzyme requires reduced ferredoxin, Fe2+-dithiol or Co2+-mercaptoethanol complexes can substitute for ferredoxin
-
NADPH
-
more effective for activation than NADPH, 0.02 mM NADPH activates over 80% inactive enzyme in cell-free extracts
Oxamate
-
obligatory component of the activation reaction
pyruvate
-
obligatory component of the activation reaction
S-adenosylmethionine
-
obligatory component of the activation reaction
S-adenosylmethionine
-
-
S-adenosylmethionine
-
-
S-adenosylmethionine
-
obligatory component of the activation reaction
Y06I
-
autonomous glycyl radical cofactor, reconstituting the catalytic center of oxygen-fragmented enzyme
-
YfiD
P09973
; autonomous glycyl radical cofactor, reconstituting the catalytic center of oxygen-fragmented enzyme
-
Ferredoxin
-
methylviologen can replace ferredoxin
-
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)
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.051
-
acetyl-CoA
-
-
0.26
-
acetyl-CoA
-
-
0.012
-
CoA
-
pyruvate
20
-
formate
-
pyruvate-formate exchange
0.6
-
pyruvate
-
pyruvate-formate exchange
0.964
-
pyruvate
-
pH 7.6, 30C, recombinant mutant A273C
2
-
pyruvate
-
-
2.05
-
pyruvate
-
-
2.37
-
pyruvate
-
pH 7.6, 30C, recombinant wild-type enzyme
2.6
-
pyruvate
-
-
3.55
-
pyruvate
-
pH 7.6, 30C, recombinant mutant E400I
3.6
-
pyruvate
-
pH 7.6, 30C, recombinant mutant E336C
24.5
-
formate
-
-
additional information
-
additional information
-
steady-state kinetics of wild-type and mutant enzymes
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3.8
-
formate
-
-
4.33
-
formate
-
backward direction
11
-
pyruvate
-
-
12.8
-
pyruvate
-
forward direction
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.42
-
methacrylate
-
pH 7.4, 30C
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
additional information
-
-, P37836
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
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-
assay at
7
7.5
-
Tris-acetate buffer
7.5
-
-
-
7.5
-
-
assay at
7.6
-
-
assay at
7.8
8.4
-
-
7.8
8.5
-
forward direction
8.5
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
8.3
-
40% of activity maximum at pH 6.5, between pH 7.0-8.3 80% of maximum activity
6.5
8.5
-, P37836
activity assay at, wild-type and mutant protein
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
assay at room temperature
30
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
35
-
activity is about 78 times of that at 22C
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
microaerobic cultures, glucose-limited chemostat cultures, different strains, growth rates, overview
Manually annotated by BRENDA team
-, P37836
formate accumulation inside anaerobically adapted Chlamydomonas reinhardtii CC-277 cells measured
Manually annotated by BRENDA team
Clostridium thermocellum 27405.
-
-
-
Manually annotated by BRENDA team
Streptococcus thermophilus LMG18311
-
-
-
Manually annotated by BRENDA team
-, P37836
formate accumulation in the medium of anaerobically adapted Chlamydomonas reinhardtii CC-277 cells measured
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Streptococcus thermophilus LMG18311
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
80000
-
-
identification of pfl gene product
85120
-
-
amino acid sequence calculation
140000
-
-
gel filtration, sedimentation velocity
150000
-
-
gel filtration
151000
-
-
sedimentation equilibrium
170000
180000
-
gel filtration
180000
-
-
TOF-MS flight mass spectrometry
297000
-
-
dynamic light scattering, analytical ultracentrifugation
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-, Q46266
2 * 85000, homodimer, SDS-PAGE
dimer
-
2 * 85000, homodimer, SDS-PAGE; 2 * 85500, homodimer, SDS-PAGE
dimer
-
2 * 70000
dimer
-
2 * 90000, SDS-PAGE
dimer
-
1 * 87000 + 1 * 83000, TOF-MS flight mass spectrometry, SDS-PAGE; 2 * 80000-90000, SDS-PAGE
dimer
O66391, -
1 * 87000 + 1 * 83000, TOF-MS flight mass spectrometry, SDS-PAGE
dimer
-
2 * 85000, homodimer, SDS-PAGE
dimer
Clostridium pasteurianum DSM525
-
2 * 85000, homodimer, SDS-PAGE
-
dimer
Escherichia coli K12
-
; 2 * 70000; 2 * 85000, homodimer, SDS-PAGE; 2 * 85000, homodimer, SDS-PAGE; 2 * 85500, homodimer, SDS-PAGE
-
dimer
-
1 * 87000 + 1 * 83000, TOF-MS flight mass spectrometry, SDS-PAGE; 1 * 87000 + 1 * 83000, TOF-MS flight mass spectrometry, SDS-PAGE; 2 * 80000-90000, SDS-PAGE
-
tetramer
-
4 * 95000, structure analysis, crystal packing, solution X-ray scattering, and ultracentrifugation
dimer
Streptococcus mutans JC2
-
2 * 90000, SDS-PAGE
-
additional information
-
secondary structure, overview
additional information
Escherichia coli JM109
-
secondary structure, overview
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
PFL-activating enzyme
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
space group P4(1)2(1)2
-
space group P4(3)2(1)2 a = b = 159 A, c = 160 A
P09373
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
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
activity decreases to less than 10% of the maximal activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
30
-
stable in anaerobic buffers for days at 0C, at 30C for several hours
30
-
-
activity declines with a half-time of 50 min
30
-
-
pH 7.5, half-lives of recombinant wild-type and mutant enzymes, overview
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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
-
virtually stable at 0C and pH 8.0 if kept in media which display a redoxpotential of 0.2 V or below
-
stable for 2 h at 35C in untreated cell-free extracts under strictly anaerobic conditions. In dialyzed cell-free extracts, activity decreases gradually.
-
unstable even when stored anaerobically
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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
immediately inactivated by exposure to the air
-
487222
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 10 mM MOPS-KOH, pH 7.0, 50 mM KCl, thiols, EDTA in 50% ethyleneglycol, proved stable for months
-
-20C, stable for at least several months
-
4C, 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%
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
native enzyme at pH 6.4, by anion exchange and hydrophobic interaction chromatography, and gel filtration, to homogeneity
-
gel filtration, Western Blot, heterologously expressed protein
-, P37836
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
-
partially
-
recombinant enzyme
P09373
recombinant His-tagged wild-type and mutant enzymes from strain BL21(DE3) by nickel affinity chromatography to homogeneity
-
centrifugation, washing in 50 mM potassium phosphate buffer, pH 7.5, resuspension, French press disruption, centrifugation of crude extract and of resulting supernatant
-
recombinant enzyme
O66391, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-, P37836
gene pfl, DNA and amino acid sequence determination and analysis, detailed phylogenetic analysis, overview
-, Q1RS83
pfl gene cloned
-, Q46266
gene pfl, DNA and amino acid sequence determination and analysis, sequence comparison
-
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 in Escherichia coli
-
overexpression of the His6-tagged enzyme as single enzyme or as AdhE-Pfl in strain BL21(DE3)
-
overproducing of the enzyme in Escherichia coli 234M1 transformed with expression vector p153E1
-
recombinant PFL expressed in Escherichia coli BL21 (DE3)
-
recombinant pfl in Escherichia coli RM220
-
recombinant pfl in Escherichia coli RM221
P09373
structural gene pfl cloned and sequenced, homologous expression and overproduction in Escherichia coli K12
-
gene deletion is transduced via Bacteriophage P1
-
pfl gene expressed under control of different constitutive promoters, PFL-deficient strain CRM40 complemented
-
gene pflB, expression analysis
-
pfl gene cloned and expressed in Escherichia coli HB101
-
PCR-amplificatioin, mariner plasmid
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
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
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
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
A273C
Escherichia coli JM109
-
site-directed mutagenesis, the mutant is less thermostable than the wild-type enzyme
-
E336C
Escherichia coli JM109
-
site-directed mutagenesis, the mutant is more thermostable than the wild-type enzyme, Tm is increased 3.7fold, half-life 1.8fold
-
E400I
Escherichia coli JM109
-
site-directed mutagenesis, the mutant is more thermostable than the wild-type enzyme, Tm is increased 2.2fold, half-life 2.21fold
-
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
-
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.
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
biotechnology
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D-lactate production for the use in biopolymer production as biodegradable alternative for oil-derived plastics
nutrition
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plays a significant role in industrial milk fermentation