Information on EC 1.97.1.4 - [formate-C-acetyltransferase]-activating enzyme

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.97.1.4
-
RECOMMENDED NAME
GeneOntology No.
[formate-C-acetyltransferase]-activating enzyme
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical
show the reaction diagram
the glycyl radical in pyruvate formate-lyase is produced by stereospecific abstraction of the pro-S hydrogen of Gly734 by the 5'-deoxyadenosine radical generated in the active center of the enzyme
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S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical
show the reaction diagram
mechanism, a deoxyadenosyl radical intermediate, generated by the reductive cleavage of S-adenosylmethionine serves as the actual H atom abstracting species
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S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical
show the reaction diagram
4Fe-4S cluster is involved in catalysis by coordinating S-adenosyl-L-methionine
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S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
[formate C-acetyltransferase]-glycine dihydroflavodoxin:S-adenosyl-L-methionine oxidoreductase (S-adenosyl-L-methionine cleaving)
An iron-sulfur protein. A single glycine residue in EC 2.3.1.54, formate C-acetyltransferase, is oxidized to the corresponding radical by transfer of H from its CH2 to AdoMet with concomitant cleavage of the latter. The reaction requires Fe2+. The first stage is reduction of the AdoMet to give methionine and the 5'-deoxyadenosin-5'-yl radical, which then abstracts a hydrogen radical from the glycine residue.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Activase, pyruvate formate-lyase
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Formate acetyltransferase activase
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Formate-lyase-activating enzyme
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PFL
P0A9N4
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PFL activase
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-
-
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PFL activating enzyme
Q6RFH6
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PFL-activating enzyme
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-
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PFL-AE
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PFL-glycine:S-adenosyl-L-methionine H transferase (flavodoxin-oxidizing, S-adenosyl-L-methionine-cleaving)
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pyruvate formate lyase activating enzyme
Q6RFH6
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Pyruvate formate-lyase activase
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Pyruvate formate-lyase activating enzyme
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pyruvate formate-lyase-activating enzyme
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CAS REGISTRY NUMBER
COMMENTARY
206367-15-9
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
induction of transcription by anaerobiosis and darkness, but little induction on protein level
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Manually annotated by BRENDA team
strain 27405. Enzyme activity is present in late log and stationary growth phase of cells grown on cellobiose
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Manually annotated by BRENDA team
Clostridium thermocellum 27405.
strain 27405. Enzyme activity is present in late log and stationary growth phase of cells grown on cellobiose
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
P0A9N4
enzyme is activated by pyruvate formate-lyase-activating enzyme by generating a catalytically essential radical on residue Gly734. In the open conformation of the enzyme, the Gly734 residue is located not in its buried position in the enzyme active site but rather in a more solvent-exposed location. The presence of the activating enzyme increases the proportion of enzyme in the open conformation. The activating enzyme accesses residue Gly734 for direct hydrogen atom abstraction by binding to the Gly734 loop in the open conformation, thereby shifting the closed open equilibrium of the enzyme to the right
physiological function
P0A9N4
pyruvate formate-lyase-activating enzyme (PFL-AE) activates pyruvate formate-lyase
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
S-Adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine
?
show the reaction diagram
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additional information
?
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P0A9N4
pyruvate formate-lyase-activating enzyme (PFL-AE) activates pyruvate formate-lyase by generating a catalytically essential radical on Gly-734 of pyruvate formate-lyase. PFL-AE shifts the closed/open formation of pyruvate formate-lyase to the open conformation, in which Gly-734 is more solvent-exposed and accessible to the PFL-AE active site
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METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Cobalt
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Co(II) and Cu(II) can be reconstituted into the protein with similar stoichiometry
copper
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Co(II) and Cu(II) can be reconstituted into the protein with similar stoichiometry
Fe2+
Q93UQ7, -
required
Iron
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[4Fe-4S]2+clusters at the subunit interface can undergoe reversible oxidative conversion to [2Fe-2S]2+clusters under conditions of incomplete anaerobicity
Iron
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contains an iron-sulfur cluster, most probably of the [4Fe-4S]type
Iron
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binds one Fe(II) per protein monomer. Co(II) and Cu(II) can be reconstituted into the protein with similar stoichiometry
Iron
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2.8 mol per mol of enzyme, as (3Fe-4S)+ cluster
Iron
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anaerobically purified enzyme, 4FE-4S cluster in a diamagnetic 2+ oxidation state
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Peptides
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peptides homologous to the Gly734 site of pyruvate formate-lyase that are active as substrates
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
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contains a covalently bound chromophoric factor which has an optical absorptiion peak at 388 nm
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KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0012
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inactive pyruvate formate-lyase
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0.0028
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S-adenosyl-L-methionine
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LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
Escherichia coli (strain K12)
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
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x * 28035, calculation from nucleotide sequence
?
Escherichia coli K12
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x * 28035, calculation from nucleotide sequence
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dimer
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2 * 28000
monomer
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1 * 29500, SDS-PAGE
monomer
Q93UQ7, -
1 * 29900, calculated, 1 * 30000, SDS-PAGE
monomer
Escherichia coli K12
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1 * 29500, SDS-PAGE
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additional information
P0A9N4
model in which the enzyme can exist in either a closed conformation, with residue Gly734 buried in the active site and harboring a stable glycyl radical, or an open conformation, with Gly734 more solvent-exposed and accessible to the activating enzyme's active site
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
clone encodes a putative protein of 8532 amino acids
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over-expressed in Escherichia coli
P0A9N4
overexpression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C102S
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mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent
C12S
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mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent
C29S
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mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent
C33S
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mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent
C36S
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mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent
C94S
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mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent