Information on EC 1.2.7.1 - pyruvate synthase

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

EC NUMBER
COMMENTARY
1.2.7.1
-
RECOMMENDED NAME
GeneOntology No.
pyruvate synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
2-oxobutanoate degradation II
-
Butanoate metabolism
-
Carbon fixation pathways in prokaryotes
-
Citrate cycle (TCA cycle)
-
Entner-Doudoroff pathway II (non-phosphorylative)
-
gluconeogenesis II (Methanobacterium thermoautotrophicum)
-
glutamate degradation VII (to butanoate)
-
glycerol degradation to butanol
-
Glycolysis / Gluconeogenesis
-
incomplete reductive TCA cycle
-
isoleucine biosynthesis IV
-
isopropanol biosynthesis
-
Metabolic pathways
-
Methane metabolism
-
Microbial metabolism in diverse environments
-
Nitrotoluene degradation
-
Propanoate metabolism
-
purine nucleobases degradation II (anaerobic)
-
pyruvate fermentation to acetate I
-
pyruvate fermentation to acetate III
-
pyruvate fermentation to acetate VI
-
pyruvate fermentation to acetate VII
-
pyruvate fermentation to acetone
-
pyruvate fermentation to butanoate
-
pyruvate fermentation to butanol I
-
pyruvate fermentation to ethanol III
-
pyruvate fermentation to hexanol
-
Pyruvate metabolism
-
reductive monocarboxylic acid cycle
-
reductive TCA cycle I
-
reductive TCA cycle II
-
SYSTEMATIC NAME
IUBMB Comments
pyruvate:ferredoxin 2-oxidoreductase (CoA-acetylating)
Contains thiamine diphosphate and [4Fe-4S] clusters. The enzyme also decarboxylates 2-oxobutyrate with lower efficiency, but shows no activity with 2-oxoglutarate. This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For examples of other members of this family, see EC 1.2.7.3, 2-oxoglutarate synthase and EC 1.2.7.7, 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ape2126/2128
Q9YA13 and Q9YA11
ordered locus name
OFOR
Q9YA13 and Q9YA11
-
PFO
Giardia intestinalis WB
Q24982
-
-
PFOR
Chlamydomonas reinhardtii CC124
-
;
-
PFR
Chlamydomonas reinhardtii CC124
-
-
-
PFR1
Chlamydomonas reinhardtii CC124
-
-
-
POR
-
bifunctional enzyme that catalyzes both the oxidative and nonoxidative decarboxylation of pyruvate
POR
Pyrococcus furiosus DSM3638
-
-
-
pyruvate ferredoxin oxidoreductase
-
-
pyruvate:ferredoxin oxidoreductase
-
-
pyruvate:ferredoxin oxidoreductase
Archaeoglobus fulgidus 7324
-
-
-
pyruvate:ferredoxin oxidoreductase
-
-
pyruvate:ferredoxin oxidoreductase
Chlamydomonas reinhardtii CC124
-
;
-
pyruvate:ferredoxin oxidoreductase
-
-
pyruvate:ferredoxin oxidoreductase
-
-
pyruvate:ferredoxin oxidoreductase
Q24982
-
pyruvate:ferredoxin oxidoreductase
Giardia intestinalis WB
Q24982
-
-
pyruvate:ferredoxin oxidoreductase
-
-
pyruvate:ferredoxin oxidoreductase
-
-
-
pyruvate:ferredoxin oxidoreductase A
-
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Q9YA13: alpha-subunit, Q9YA11: beta-subunit
Q9YA13 and Q9YA11
-
Manually annotated by BRENDA team
Archaeoglobus fulgidus 7324
-
-
-
Manually annotated by BRENDA team
Archaeoglobus lithotrophicus TF-2
-
-
-
Manually annotated by BRENDA team
Chlamydomonas reinhardtii CC124
-
-
-
Manually annotated by BRENDA team
Giardia intestinalis WB
-
UniProt
Manually annotated by BRENDA team
Pyrococcus furiosus DSM3638
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
resistance to metronidazole is associated with enzyme down-regulation
physiological function
-
PFOR is translated after the second phase of the excystation process
physiological function
-
Archaeoglobus fulgidus strain 7324 converts starch to acetate via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming)
physiological function
-
the enzyme is a surface-associated cell-binding protein that lacks enzyme activity and is involved in cytoadherence to host cells
physiological function
Archaeoglobus fulgidus 7324
-
Archaeoglobus fulgidus strain 7324 converts starch to acetate via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming)
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxo-4-methyl-thio-butyrate + CoA + 2 methyl viologen
?
show the reaction diagram
-, Q9YA13 and Q9YA11
enzyme Ape2126/2128, 37% of the activity compared to pyruvate
-
-
?
2-oxoadipate + CoA + 2 methyl viologen
?
show the reaction diagram
-, Q9YA13 and Q9YA11
enzyme Ape2126/2128, 37% of the activity compared to pyruvate
-
-
?
2-oxobutyrate + CoA + 2 oxidized methyl viologen
propanoyl-CoA + CO2 + 2 reduced methyl viologen
show the reaction diagram
-, Q9YA13 and Q9YA11
enzyme Ape2126/2128, 98% of the activity compared to pyruvate
-
-
?
2-oxobutyrate + CoA + oxidized methyl viologen
propanoyl-CoA + CO2 + reduced methyl viologen
show the reaction diagram
-
the enzyme reacts with 2-oxobutyrate and oxaloacetate at 38% activity relative to the activity against pyruvate
-
-
?
2-oxobutyrate + CoA + oxidized methyl viologen
propanoyl-CoA + CO2 + reduced methyl viologen
show the reaction diagram
-
the enzyme reacts with oxaloacetate at 4.8 activity relative to the activity against pyruvate
-
-
?
2-oxobutyrate + CoA + oxidized methyl viologen
propanoyl-CoA + CO2 + reduced methyl viologen
show the reaction diagram
-
the enzyme reacts with 2-oxobutyrate and oxaloacetate at 38% activity relative to the activity against pyruvate
-
-
?
glyoxylate + CoA + 2 oxidized methyl viologen
?
show the reaction diagram
-, Q9YA13 and Q9YA11
enzyme Ape2126/2128, 89% of the activity compared to pyruvate
-
-
?
oxaloacetate + CoA + oxidized methyl viologen
?
show the reaction diagram
-
the enzyme reacts with 2-oxobutyrate and oxaloacetate at 38% activity relative to the activity against pyruvate
-
-
?
oxaloacetate + CoA + oxidized methyl viologen
?
show the reaction diagram
-
the enzyme reacts with oxaloacetate at 40% activity relative to the activity against pyruvate
-
-
?
oxaloacetate + CoA + oxidized methyl viologen
?
show the reaction diagram
-
the enzyme reacts with 2-oxobutyrate and oxaloacetate at 38% activity relative to the activity against pyruvate
-
-
?
oxaloacetate + CoA + oxidized methyl viologen
? + reduced methyl viologen + H+
show the reaction diagram
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii CC124
-
-
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
-
-
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
-
-
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
-
-
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
-
Archaeoglobus fulgidus strain 7324 converts starch to acetate via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming)
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
-
ferredoxin is an electron donor for the enzyme reaction in vivo
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
-
the enzyme catalyzes the final oxidative step in carbohydrate fermentation in which pyruvate is oxidized to acetyl-CoA and CO2, coupled to the reduction of ferredoxin
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
-
no activity with NAD+ or NADP+ as electron aceptor
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
-
pyruvate ferredoxin oxidoreductase functions as a CoA-dependent pyruvate decarboxylase. Ferredoxin is not necessary for the pyruvate decarboxylase activity of POR. At 80C (pH 8.0), the apparent Vm value for pyruvate decarboxylation is about 40% of the apparent Vm value for pyruvate oxidation rate (using Pyrococcus furiosus ferredoxin as the electron acceptor)
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
-
the ability of the 4Fe-ferredoxin to accept electrons is not absolutely dependent upon Asp14 (of ferredoxin), as this residue can be effectively replaced by Cys. However, the efficiency of electron transfer is compromised if Asp14 is replaced by Ser, or if the 4Fe-cluster is converted to the 3Fe-form, but Asp14 does not appear to offer any kinetic advantage over the expected Cys
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
-
ferredoxin is an electron donor for the enzyme reaction in vivo
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
Pyrococcus furiosus DSM3638
-
the ability of the 4Fe-ferredoxin to accept electrons is not absolutely dependent upon Asp14 (of ferredoxin), as this residue can be effectively replaced by Cys. However, the efficiency of electron transfer is compromised if Asp14 is replaced by Ser, or if the 4Fe-cluster is converted to the 3Fe-form, but Asp14 does not appear to offer any kinetic advantage over the expected Cys
-
-
?
pyruvate + CoA + 2 oxidized methyl viologen
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
show the reaction diagram
-, Q9YA13 and Q9YA11
enzyme Ape2126/2128
-
-
?
pyruvate + CoA + benzyl viologen
acetyl-CoA + CO2 + reduced benzyl viologen
show the reaction diagram
-
-
-
-
?
pyruvate + CoA + FMN
acetyl-CoA + CO2 + FMNH + H+
show the reaction diagram
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii CC124
-
5-6times lower activity with FMN as compared to benzyl viologen
-
-
?
pyruvate + CoA + oxidized benzyl viologen
acetyl-CoA + CO2 + reduced benzyl viologen + H+
show the reaction diagram
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii CC124
-
best activity with benzyl viologen
-
-
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
show the reaction diagram
-
-
-
-
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
show the reaction diagram
-
-
-
-
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
show the reaction diagram
-
-
-
-
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
show the reaction diagram
Giardia intestinalis, Giardia intestinalis WB
Q24982
-
-
-
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
show the reaction diagram
Chlamydomonas reinhardtii CC124
-
-
-
-
?
pyruvate + CoA + oxidized ferredoxin 1
acetyl-CoA + CO2 + reduced ferredoxin 1 + H+
show the reaction diagram
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii CC124
-
-
-
-
?
pyruvate + CoA + oxidized ferredoxin 2
acetyl-CoA + CO2 + reduced ferredoxin 2 + H+
show the reaction diagram
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii CC124
-
-
-
-
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen
show the reaction diagram
-
-
-
-
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen
show the reaction diagram
-
-
-
-
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen
show the reaction diagram
-
specific activity with methyl viologen is 10fold higher compared to the specific activity with Hydrogenobacter thermophilus ferredoxin
-
-
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen
show the reaction diagram
-
the enzyme does not catalyze the oxidation of 2-oxoglutarate, indolepyruvate, phenylpyruvate, glyoxylate, and hydroxypyruvate
-
-
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen
show the reaction diagram
-
specific activity with methyl viologen is 10fold higher compared to the specific activity with Hydrogenobacter thermophilus ferredoxin
-
-
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen + H+
show the reaction diagram
-
-
-
-
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen + H+
show the reaction diagram
-
3-4times lower activity with methyl viologen as compared to benzyl viologen
-
-
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen + H+
show the reaction diagram
Chlamydomonas reinhardtii CC124
-
-
-
-
?
pyruvate + CoA + oxidized methylene blue
acetyl-CoA + CO2 + reduced methylene blue + H+
show the reaction diagram
-
2.5-3times lower activity with methylene blue as compared to benzyl viologen
-
-
?
pyruvate + CoA + oxidized nitro blue tetrazolium
acetyl-CoA + CO2 + reduced nitro blue tetrazolium + H+
show the reaction diagram
-
-
-
-
?
hydroxypyruvate + CoA + 2 methyl viologen
?
show the reaction diagram
-, Q9YA13 and Q9YA11
enzyme Ape2126/2128, 38% of the activity compared to pyruvate
-
-
?
additional information
?
-
-, Q9YA13 and Q9YA11
activity with 2-oxoglutarate is 6% compared to the activity with pyruvate. No activity with 3-methyl-2-oxovalerate, 4-methyl-2-oxovalerate, 2-oxoisocaproic acid or 2-oxooctanoic acid, enzyme Ape2126/2128,
-
-
-
additional information
?
-
-
no activity with 2-oxoglutarate, oxomalonate, 2-oxoisocaproate, phosphoenolpyruvate, indole-3-pyruvate, or phenylpyruvate
-
-
-
additional information
?
-
-
no activity with 2-oxoglutarate, oxomalonate, 2-oxoisocaproate, phosphoenolpyruvate, indole-3-pyruvate, or phenylpyruvate
-
-
-
additional information
?
-
-
no activity with 2-oxoglutarate, phenyl pyruvate or indole pyruvate
-
-
-
additional information
?
-
-
the enzyme cannot use 2-oxoglutarate as substrate, the enzyme is able to transfer electrons from pyruvate to the [Fe-Fe]-hydrogenase HYDA1, using the ferredoxins PETF and FDX2 as electron carriers
-
-
-
additional information
?
-
-
neither NAD+ nor NADP+ can be reduced by the enzyme
-
-
-
additional information
?
-
-
no activity with 2-oxoglutarate, oxomalonate, 2-oxoisocaproate, phosphoenolpyruvate, indole-3-pyruvate, or phenylpyruvate
-
-
-
additional information
?
-
Chlamydomonas reinhardtii CC124
-
the enzyme cannot use 2-oxoglutarate as substrate, the enzyme is able to transfer electrons from pyruvate to the [Fe-Fe]-hydrogenase HYDA1, using the ferredoxins PETF and FDX2 as electron carriers
-
-
-
additional information
?
-
Chlamydomonas reinhardtii CC124
-
neither NAD+ nor NADP+ can be reduced by the enzyme
-
-
-
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
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
-
-
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
-
-
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
-
Archaeoglobus fulgidus strain 7324 converts starch to acetate via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming)
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
-
ferredoxin is an electron donor for the enzyme reaction in vivo
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
-
the enzyme catalyzes the final oxidative step in carbohydrate fermentation in which pyruvate is oxidized to acetyl-CoA and CO2, coupled to the reduction of ferredoxin
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
-
ferredoxin is an electron donor for the enzyme reaction in vivo
-
-
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
show the reaction diagram
-
-
-
-
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
show the reaction diagram
-
-
-
-
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
show the reaction diagram
-
-
-
-
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
show the reaction diagram
Giardia intestinalis, Giardia intestinalis WB
Q24982
-
-
-
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
show the reaction diagram
Chlamydomonas reinhardtii CC124
-
-
-
-
?
pyruvate + CoA + oxidized ferredoxin 1
acetyl-CoA + CO2 + reduced ferredoxin 1 + H+
show the reaction diagram
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii CC124
-
-
-
-
?
pyruvate + CoA + oxidized ferredoxin 2
acetyl-CoA + CO2 + reduced ferredoxin 2 + H+
show the reaction diagram
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii CC124
-
-
-
-
?
additional information
?
-
-
the enzyme cannot use 2-oxoglutarate as substrate, the enzyme is able to transfer electrons from pyruvate to the [Fe-Fe]-hydrogenase HYDA1, using the ferredoxins PETF and FDX2 as electron carriers
-
-
-
additional information
?
-
Chlamydomonas reinhardtii CC124
-
the enzyme cannot use 2-oxoglutarate as substrate, the enzyme is able to transfer electrons from pyruvate to the [Fe-Fe]-hydrogenase HYDA1, using the ferredoxins PETF and FDX2 as electron carriers
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
thiamine diphosphate
-
0.5-0.7 per mol of enzyme
thiamine diphosphate
-
per mol, the enzyme contains 0.8 mol thiamine diphosphate
thiamine diphosphate
-
essential cofactor, upon addition of Mg2+, an ion that stabilizes thiamine diphosphate, the enzymatic activity almost doubles
[4Fe-4S]-center
-
the enzyme contains at least two [4Fe-4S] clusters. The purified and reconstituted delta subunit contains 8 Fe mol/mol
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Iron
-
8.3 gatoms/100000 g of protein
Iron
-
per mol, the enzyme contains 9 mol of non-heme iron, and 8 mol of acid-labile sulfur. No inhibition by sodium arsenite
Iron
-
the enzyme contains at least two [4Fe-4S] clusters. The purified and reconstituted delta subunit contains 8 Fe mol/mol
Mg2+
-
upon addition of Mg2+, an ion that stabilizes thiamine diphosphate, the enzymatic activity almost doubles
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
carbon monoxide
-
0.0072 mM, 50% inhibition
dioxygen
-
the enzyme is inactivated by dioxygen. Less than 50% of the original activity remains when the protein (0.23 mg/ml in 50 mM Tris/HCl pH 7.5) is exposed to air for 80 min at 25C. Attempts to reactivate the enzyme by anoxic incubation in the presence of 2 mM dithiothreitol fail
KCl
-
0.5 M, 50% inhibition
NaCl
-
the addition of 0.3 M NaCl causes a significant inhibition (up to 80%) of the activity
KCl
-, Q9YA13 and Q9YA11
1020% inhibition is observed with 50 mM KCl, while with higher concentrations (maximum, 0.6 M), 4665% activation is reached, and further increased concentrations of KCl are inhibitory, enzyme Ape2126/2128
additional information
-
the enzyme is not inhibited by sodium nitrite (50 mM) or carbon monoxide (100% CO as gas phase)
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
thioredoxin 1
-
the Desulfovibrio vulgaris thioredoxin1 system activates the enzyme
additional information
-
dithiothreitol has no influence on the activity
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0052
-
CoA
-
in 25 mM potassium phosphate buffer (pH 7.0), 0.2 mM thiamine diphosphate, 1 mM MgCl2, at 25 C
0.02
-
CoA
-
pH 7.5, 65C
0.054
-
CoA
-
pH 7.6, 70C
0.11
-
CoA
-
pH 8.4, 80C
0.01
-
oxidized ferredoxin
-
pH 7.5, 65C
0.094
-
oxidized ferredoxin
-
pH 8.4, 80C
0.0046
-
oxidized ferredoxin 1
-
in 25 mM potassium phosphate buffer (pH 7.0), 0.2 mM thiamine diphosphate, 1 mM MgCl2, at 25 C
-
0.0037
-
oxidized ferredoxin 2
-
in 25 mM potassium phosphate buffer (pH 7.0), 0.2 mM thiamine diphosphate, 1 mM MgCl2, at 25 C
-
2.33
-
oxidized methyl viologen
-
in 100 mM potassium phosphate buffer, pH 6.8, temperature not specified in the publication
0.16
-
pyruvate
-
in 25 mM potassium phosphate buffer (pH 7.0), 0.2 mM thiamine diphosphate, 1 mM MgCl2, at 25 C
0.24
-
pyruvate
-, Q9YA13 and Q9YA11
pH 8.5, 80C, enzyme Ape2126/2128
0.3
-
pyruvate
-
pH 7.5, 65C
0.46
-
pyruvate
-
pH 8.4, 80C
1.65
-
pyruvate
-
in 100 mM potassium phosphate buffer, pH 6.8, temperature not specified in the publication
3.45
-
pyruvate
-
pH 7.6, 70C
0.67
-
CoA
-
in 100 mM potassium phosphate buffer, pH 6.8, temperature not specified in the publication
additional information
-
additional information
-
pH 8.0, 80C, kinetic parameters for the native and mutant forms of Pyrococcus furiosus ferredoxin
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
7.2
-
pyruvate
-
80C, pH 7.5, mutant enzyme Y253F
16065
20
-
pyruvate
-
80C, pH 7.5, mutant enzyme I255L
16065
21
-
pyruvate
-
80C, pH 7.5, mutant enzyme P254G
16065
24
-
pyruvate
-
80C, pH 7.5, mutant enzyme I255V
16065
25
-
pyruvate
-
80C, pH 7.5, mutant enzyme I255S
16065
28
-
pyruvate
-
80C, pH 7.5, mutant enzyme T256V
16065
31
-
pyruvate
-
80C, pH 7.5, mutant enzyme T256A
16065
38
-
pyruvate
-
80C, pH 7.5, mutant enzyme T256S
16065
41
-
pyruvate
-
80C, pH 7.5, mutant enzyme I255M
16065
145.5
-
pyruvate
-
80C, pH 7.5, recombinant enzyme
16065
204
-
pyruvate
-
80C, pH 7.5, natural enzyme
16065
additional information
-
additional information
-
pH 8.0, 80C, kinetic parameters for the native and mutant forms of Pyrococcus furiosus ferredoxin
0
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
11
-
nitrite
-
pH 8.4, 80C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.04
-
-
pH 7.5, 65C, cell extract
0.06
-
-
pH 7.5, 65C, cell extract
0.13
-
-
50C, pH not specified in the publication, enzyme from lactate-grown cells
0.4
-
-
using cytochrome c as electron acceptor, in 25 mM potassium phosphate buffer (pH 7.0), 0.2 mM thiamine diphosphate, 1 mM MgCl2, at 25 C
0.7
-
-
pH 7.5, 65C, cell extract
2.3
-
-
using FMN as electron acceptor, in 25 mM potassium phosphate buffer (pH 7.0), 0.2 mM thiamine diphosphate, 1 mM MgCl2, at 25 C
3.46
-
-
pH 7.6, 70C
3.7
-
-
using methyl viologen as electron acceptor, in 25 mM potassium phosphate buffer (pH 7.0), 0.2 mM thiamine diphosphate, 1 mM MgCl2, at 25 C
4.5
-
-
using spinach ferredoxin 1 as electron acceptor, in 25 mM potassium phosphate buffer (pH 7.0), 0.2 mM thiamine diphosphate, 1 mM MgCl2, at 25 C
4.7
-
-
using methylene blue as electron acceptor, in 25 mM potassium phosphate buffer (pH 7.0), 0.2 mM thiamine diphosphate, 1 mM MgCl2, at 25 C
6.3
-
-
using Chlamydomonas reinhardtii ferredoxin 1 as electron acceptor, in 25 mM potassium phosphate buffer (pH 7.0), 0.2 mM thiamine diphosphate, 1 mM MgCl2, at 25 C
12
-
-
using benzyl viologen as electron acceptor, in 25 mM potassium phosphate buffer (pH 7.0), 0.2 mM thiamine diphosphate, 1 mM MgCl2, at 25 C
20
-
-
pH 8.4, 80C
40
-
-
pH 7.5, 25C
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
7.5
-
recombinant enzyme, in 25 mM potassium phosphate
8
-
-, Q9YA13 and Q9YA11
enzyme Ape2126/2128
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
8.5
-
pH 5.5: about 60% of maximal activity, pH 8.5: about 35% of maximal activity
6
10
-, Q9YA13 and Q9YA11
pH 6.0: about 45% of maximal activity, pH 10.0: about 60% of maximal activity, enzyme Ape2126/2128
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50
-
-
assay at
80
-
-, Q9YA13 and Q9YA11
assay at
105
-
-, Q9YA13 and Q9YA11
enzyme Ape2126/2128
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
80
110
-, Q9YA13 and Q9YA11
80C: 45% of maximal activity, 110C: 95% of maximal activity, enzyme Ape2126/2128
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Chlamydomonas reinhardtii CC124
-
-
-
Manually annotated by BRENDA team
-
about 1% of activity detected in cytosol
Manually annotated by BRENDA team
-
80% of activity detected in hydrogenosome
Manually annotated by BRENDA team
-
about 4% of activity detected in membrane
Manually annotated by BRENDA team
Giardia intestinalis WB
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
100000
-
-
electrophoresis on non-denaturing gels
110000
-
-, Q9YA13 and Q9YA11
gel filtration, enzyme Ape2126/2128
120000
-
-
gel filtration
125000
-
-
polyacrylamide gradient gel electrophoresis
135000
-
-
gel filtration
235000
-
-
recombinant enzyme, native PAGE
280000
-
-
dimer, non-denaturing gradient gel in absence of reducing agent
545000
-
-
tetramer, non-denaturing gradient gel in absence of reducing agent
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 144000, SDS-PAGE
?
Q24982
x * 140000, SDS-PAGE
?
-
x * 120000, pyruvate : ferredoxin oxidoreductase A, SDS-PAGE
?
Chlamydomonas reinhardtii CC124
-
x * 144000, SDS-PAGE
-
?
Giardia intestinalis WB
-
x * 140000, SDS-PAGE
-
heterodimer
-, Q9YA13 and Q9YA11
1 * 71639 + 1 * 34936, calculated from sequence, enzyme Ape2126/2128; 1 * 72000 + 1 * 35000, SDS-PAGE, enzyme Ape2126/2128
homodimer
-
2 * 130000, SDS-PAGE
tetramer
-
1 * 45000 + 1 * 33000 + 1 * 25000 + 1 * 13000, SDS-PAGE
tetramer
-
1 * 46000 + 1 * 31500 + 1 * 29000 + 1 * 24500, SDS-PAGE
tetramer
-
1 * 46000 + 1 * 31500 + 1 * 29000 + 1 * 24500, SDS-PAGE
-
trimer
-
1 * 45000 + 1 * 31000 + 1 * 24000, SDS-PAGE
homodimer
Chlamydomonas reinhardtii CC124
-
2 * 130000, SDS-PAGE
-
additional information
-
the enzyme is composed of two catalytic units of molecular mass 120000 Da. Each unit consists of four subunits, alpha/beta/gamma/delta, with masses of approximately 44000 Da, 36000 Da, 20000 Da, and 12000 Da, respectively, and contains at least two [4Fe-4S] clusters. The recombinantly expressed and reconstituted delta subunit is monomeric with a mass of 11879 Da
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
55
-
-
1 h, stable
70
-
-
8 h, anoxic conditions, 50% loss of activity
75
-
-
30 min, anoxic conditions, more than 80% residual activity after heating
80
-
-
50% loss of activity after 23 min
80
-
-, Q9YA13 and Q9YA11
20 min, stable, enzyme Ape2126/2128
85
-
-
the recombinantly expressed, purified and reconstituted delta subunit is stable for 2 h
90
-
-
50% loss of activity after 18 min
90
-
-
60 min, in the presence of 2 M KCl, 50% loss of activity. In absence of salt 50% loss of activity after 50 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purified enzyme, stored for one year under liquid N2, no loss of activity if thawed anaerobically
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the enzyme is inactivated by O2. Less than 50% of the original activity remains when the protein (0.23 mg/ml in 50 mM Tris/HCl pH 7.5) is exposed to air for 80 min at 25C. Attempts to reactivate the enzyme by anoxic incubation in the presence of 2 mM dithiothreitol fail
-
288449
when the recombinant enzyme (in 50 mM Tricine, pH 8.0) is exposed to air for 1 h on ice, a drastic loss of activity is observed
-
726231
the enzyme is efficiently protected when cells are exposed to air or H2O2
-
725463
the enzyme is inactivated by oxygen, which makes it difficult to purify the enzyme under oxic conditions. The enzyme can be stabilized when 0.1% Triton X-100 is added to the purification buffers
-
721444
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-70C, anaerobically in presence of CoASH, thiamine diphosphate anfd Mg2+, enzyme concentration below 0.02 mg/ml, stable for months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
enzyme Ape2126/2128
-, Q9YA13 and Q9YA11
Ni-NTA column chromatography
-
nickel affinity column chromatography
-
DE52 column chromatography, DEAE-cellulose column chromatography, and Sephadex G25 gel filtration
-
gel filtration
Q24982
recombinantly expressed delta subunit is purified after reconstitution with iron and sulfide. The reconstituted delta-subunit is monomeric with a mass of 11879 Da as determined by mass spectrometry. The purified and reconstituted delta subunit contains 8 Fe mol/mol and remains intact when incubated at 85 C for 2 h
-
Ni-NTA column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli, enzyme Ape2126/2128
-, Q9YA13 and Q9YA11
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21 cells
Q24982
the gene encoding the delta-subunit is expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
metronidazole-resistant Giardia line 106-2ID10 has decreased PFOR activity
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
biotechnology
-
pyruvate:ferredoxin oxidoreductase PFR1 and [Fe-Fe]-hydrogenase HYDA1 of Chlamydomonas can be coupled for pyruvate-dependent H2 production
biotechnology
Chlamydomonas reinhardtii CC124
-
pyruvate:ferredoxin oxidoreductase PFR1 and [Fe-Fe]-hydrogenase HYDA1 of Chlamydomonas can be coupled for pyruvate-dependent H2 production
-