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 hide
1.97.1.4
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RECOMMENDED NAME
GeneOntology No.
[formate-C-acetyltransferase]-activating enzyme
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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.
CAS REGISTRY NUMBER
COMMENTARY hide
206367-15-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
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
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
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Swissprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine
5'-deoxyadenosine + methionine + flavodoxin + formate acetyltransferase-glycine-2-yl-radical
show the reaction diagram
S-Adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine
?
show the reaction diagram
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S-adenosyl-L-methionine + NADH + formate acetyltransferase-glycine
5'-deoxyadenosine + methionine + NAD+ + formate acetyltransferase-glycine-2-yl-radical
show the reaction diagram
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40% of activity with reduced methyl viologen
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?
S-adenosyl-L-methionine + NADPH + formate acetyltransferase-glycine
5'-deoxyadenosine + methionine + NADP+ + formate acetyltransferase-glycine-2-yl-radical
show the reaction diagram
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95% of activity with reduced methyl viologen
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?
S-adenosyl-L-methionine + reduced methyl viologen + formate acetyltransferase-glycine
5'-deoxyadenosine + methionine + methyl viologen + formate acetyltransferase-glycine-2-yl-radical
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
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[4Fe-4S]-center
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an increase in pre-edge intensity is due to additional contributions from sulfide and thiolate of the Fe4S4 cluster into the C-S sigma* orbital. There is a backbonding interaction between the Fe4S4 cluster and C-S sigma* orbitals of S-adenosyl-L-methionine in this inner sphere complex. This backbonding is enhanced in the reduced form and this configurational interaction between the donor and acceptor orbitals facilitates the electron transfer from the cluster to S-adenosyl-L-methionine, that otherwise has a large outer sphere electron transfer barrier. The energy of the reductive cleavage of the C-S bond is sensitive to the dielectric of the protein in the immediate vicinity of the site as a high dielectric stabilizes the more charge separated reactant increasing the reaction barrier
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
COMMENTARY hide
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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0012
inactive pyruvate formate-lyase
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0.0028
S-adenosyl-L-methionine
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43
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25C, pH 8.1
105
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pH 6.8, 30C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.7
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20% of activity at pH 6.8
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
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isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
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gel filtration
30000
gel filtration
34000
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gel filtration
40000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 28000
monomer
additional information
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
modeling of the complex between pyruvate formate-lyase activating enzyme and flavodoxin. In the pyruvate formate-lyase activating enzyme/flavodoxin complex, FMN is located 10.7 A from the [4Fe-4S] cluster in pyruvate formate-lyase activating enzyme. The flavodoxin binding site on pyruvate formate-lyase activating enzyme is the only location other than the pyruvate formate-lyase binding site where the [4Fe-4S] cluster is close to the surface of the enzyme, which would be necessary for efficient electron transfer
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, presence of Fe(SO4)2(NH4)2 and dithiothreitol, relatively stable
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using strictly anaerobic conditions
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
clone encodes a putative protein of 8532 amino acids
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over-expressed in Escherichia coli
overexpression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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in dental plaque, under anaerobic conditions, enzyme is always kept active
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