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
LITERATURE
pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2-oxobutanoate degradation II
-
-
acetate fermentation
-
-
Butanoate metabolism
-
-
Carbon fixation pathways in prokaryotes
-
-
Citrate cycle (TCA cycle)
-
-
Entner-Doudoroff pathway II (non-phosphorylative)
-
-
gluconeogenesis II (Methanobacterium thermoautotrophicum)
-
-
glycerol degradation to butanol
-
-
Glycolysis / Gluconeogenesis
-
-
incomplete reductive TCA cycle
-
-
isopropanol biosynthesis
-
-
L-glutamate degradation VII (to butanoate)
-
-
L-isoleucine biosynthesis IV
-
-
Metabolic pathways
-
-
Methane metabolism
-
-
Microbial metabolism in diverse environments
-
-
Nitrotoluene degradation
-
-
Propanoate metabolism
-
-
purine 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).
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
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
Q9P9E5: subunit alpha, Q9P9E4: subunit beta, Q9P9E6: subunit gamma, Q9P9E7: subunit delta, Q9P9E3: subunit PorE
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
SwissProt
Manually annotated by BRENDA team
Methanococcus maripaludis DSMZ 2067
Q9P9E5: subunit alpha, Q9P9E4: subunit beta, Q9P9E6: subunit gamma, Q9P9E7: subunit delta, Q9P9E3: subunit PorE
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
SwissProt
Manually annotated by BRENDA team
P80521: subunit A, P80522: subunit B, P80523: subunit C, P80524: subunit D
P80521 and P80522 and P80523 and P80524
SwissProt
Manually annotated by BRENDA team
Methanosarcina barkeri DSM 804
-
-
-
Manually annotated by BRENDA team
Methanosarcina barkeri DSM 804
P80521: subunit A, P80522: subunit B, P80523: subunit C, P80524: subunit D
P80521 and P80522 and P80523 and P80524
SwissProt
Manually annotated by BRENDA team
W8CQR1: subunit alpha, W8CQB2: subunit beta, W8CQB1: subunit gamma, W8CR61: subunit delta
W8CQR1 and W8CQB2 and W8CQB1 and W8CR61
UniProt
Manually annotated by BRENDA team
W8CQR1: subunit alpha, W8CQB2: subunit beta, W8CQB1: subunit gamma, W8CR61: subunit delta
W8CQR1 and W8CQB2 and W8CQB1 and W8CR61
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
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
P80521 and P80522 and P80523 and P80524
first enzyme of pyruvate catabolism
physiological function
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
in autotrophic methanogens, pyruvate oxidoreductase plays a key role in the assimilation of CO2 and the biosynthesis of organic carbon
physiological function
Methanococcus maripaludis DSMZ 2067
-
in autotrophic methanogens, pyruvate oxidoreductase plays a key role in the assimilation of CO2 and the biosynthesis of organic carbon
-
physiological function
Methanosarcina barkeri DSM 804
-
first enzyme of pyruvate catabolism
-
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
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 benzyl viologen
propanoyl-CoA + CO2 + 2 oxidized benzyl viologen
show the reaction diagram
Methanosarcina barkeri, Methanosarcina barkeri DSM 804
P80521 and P80522 and P80523 and P80524
coenzyme F420 is not reduced by the purified enzyme
-
-
?
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
Methanococcus maripaludis, Methanococcus maripaludis DSMZ 2067
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 2400032000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
-
-
?
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
-
-
?
hydroxypyruvate + CoA + 2 methyl viologen
?
show the reaction diagram
Q9YA13 and Q9YA11
enzyme Ape2126/2128, 38% 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
Methanococcus maripaludis, Methanococcus maripaludis DSMZ 2067
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 2400032000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
-
-
?
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 benzyl viologen
acetyl-CoA + CO2 + 2 reduced benzyl viologen
show the reaction diagram
Methanosarcina barkeri, Methanosarcina barkeri DSM 804
P80521 and P80522 and P80523 and P80524
coenzyme F420 is not reduced by the purified enzyme
-
-
?
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
W8CQR1 and W8CQB2 and W8CQB1 and W8CR61
-
-
-
?
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
P80521 and P80522 and P80523 and P80524
first enzyme of pyruvate catabolism
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
P80521 and P80522 and P80523 and P80524
ferredoxin from Clostridium pasteurianum
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
Methanococcus maripaludis, Methanococcus maripaludis DSMZ 2067
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 2400032000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
Methanosarcina barkeri DSM 804
P80521 and P80522 and P80523 and P80524
first enzyme of pyruvate catabolism, ferredoxin from Clostridium pasteurianum
-
-
?
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
W8CQR1 and W8CQB2 and W8CQB1 and W8CR61
-
-
-
?
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 + 2 oxidized methyl viologen
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
show the reaction diagram
Methanococcus maripaludis, Methanococcus maripaludis DSMZ 2067
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 2400032000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
-
-
?
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
-
-
-
-
?
indol-3 pyruvate + CoA + 2 oxidized methyl viologen
?
show the reaction diagram
Methanococcus maripaludis, Methanococcus maripaludis DSMZ 2067
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 2400032000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
-
-
?
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
?
-
Methanosarcina barkeri, Methanosarcina barkeri DSM 804
P80521 and P80522 and P80523 and P80524
the enzyme does not catalyze the oxidation of 2-oxoglutarate, indolepyruvate, phenylpyruvate, glyoxylate, 3-hydroxypyruvate and oxaloacetate
-
-
-
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
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
W8CQR1 and W8CQB2 and W8CQB1 and W8CR61
-
-
-
?
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
Methanosarcina barkeri, Methanosarcina barkeri DSM 804
P80521 and P80522 and P80523 and P80524
first enzyme of pyruvate catabolism
-
-
?
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
W8CQR1 and W8CQB2 and W8CQB1 and W8CR61
-
-
-
?
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
COMMENTARY
LITERATURE
IMAGE
FAD
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
it is possible that flavins play an important regulatory or structural role in the enzyme
thiamine diphosphate
-
0.5-0.7 per mol of enzyme
thiamine diphosphate
P80521 and P80522 and P80523 and P80524
contains 1 mol thiamine diphosphate 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
FMN
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
it is possible that flavins play an important regulatory or structural role in the enzyme
additional information
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
the enzyme is not coenzyme F420-dependent
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4Fe-4S cluster
-
the enzyme contains three [4Fe-4S]2+/1+ clusters all with very low reduction potentials
Iron
-
8.3 gatoms/100000 g of protein
Iron
P80521 and P80522 and P80523 and P80524
contains about 12 mol of non-heme iron per mol of enzyme
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
Iron-sulfur cluster
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
porE encodes the 21500 Da subunit that contains a high cysteinyl residue content and a motif indicative of a [FeS] cluster. Subunit porF also also has a high cysteinyl residue content, and two [FeS] cluster motifs. Based upon these results, it is proposed that PorE and PorF are components of a specialized system required to transfer low-potential electrons for pyruvate biosynthesis
Mg2+
-
upon addition of Mg2+, an ion that stabilizes thiamine diphosphate, the enzymatic activity almost doubles
INHIBITORS
ORGANISM
UNIPROT
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
Dithionite
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
with 5 mM dithionite, the half-life is 7 h at 2 C, with about 90% of the original activity being lost after 24 h
glyoxylate
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
20 mM, about 40% of the original activity is lost. 2 mM glyoxylate inhibits 6%
KCl
-
0.5 M, 50% inhibition
NaCl
-
the addition of 0.3 M NaCl causes a significant inhibition (up to 80%) of the activity
oxygen
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
-
Sodium nitrite
P80521 and P80522 and P80523 and P80524
-
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)
-
additional information
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
no substrate inhibition with CoA up to 0.1 mM. Slightly or not inhibited at all by glyoxylate, nitrite, CO or potential physiological effectors. Not inhibited by CO. Potential affectors such as ATP, ADP, AMP, cAMP, GTP, GDP, GMP, NAD+, NADH, and glyceraldehyde 3-phosphate, at concentrations of 2 mM, do not affect the activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphate
P80521 and P80522 and P80523 and P80524
the purified enzyme is slightly stimulated by high phosphate concentrations. Addition of 200 mM potassium (or sodium) phosphate stimulates the enzyme activity 3-4fold
thioredoxin 1
-
the Desulfovibrio vulgaris thioredoxin1 system activates the enzyme
additional information
-
dithiothreitol has no influence on the activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.205
2-oxobutyrate
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
pH 8.6, 37C
0.0052
CoA
-
in 25 mM potassium phosphate buffer (pH 7.0), 0.2 mM thiamine diphosphate, 1 mM MgCl2, at 25 C
0.0058
CoA
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
pH 8.6, 37C
0.006
CoA
P80521 and P80522 and P80523 and P80524
37C, pH 7.0
0.02
CoA
-
pH 7.5, 65C
0.02
CoA
W8CQR1 and W8CQB2 and W8CQB1 and W8CR61
pH 8.4, 80C
0.054
CoA
-
pH 7.6, 70C
0.11
CoA
-
pH 8.4, 80C
0.264
oxaloacetate
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
pH 8.6, 37C
0.07
Oxidized benzyl viologen
P80521 and P80522 and P80523 and P80524
37C, pH 7.0
0.01
oxidized ferredoxin
-
pH 7.5, 65C
0.03
oxidized ferredoxin
P80521 and P80522 and P80523 and P80524
37C, pH 7.0, ferredoxin from Clostridium pasteurianum
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
0.07
pyruvate
P80521 and P80522 and P80523 and P80524
37C, pH 7.0
0.115
pyruvate
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
pH 8.6, 37C
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
0.25
pyruvate
W8CQR1 and W8CQB2 and W8CQB1 and W8CR61
pH 8.4, 80C
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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
13
2-oxobutyrate
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
pH 8.6, 37C
18
oxaloacetate
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
pH 8.6, 37C
27
pyruvate
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
pH 8.6, 37C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
68.2
oxaloacetate
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
pH 8.6, 37C
57
7.2
pyruvate
-
80C, pH 7.5, mutant enzyme Y253F
31
20
pyruvate
-
80C, pH 7.5, mutant enzyme I255L
31
21
pyruvate
-
80C, pH 7.5, mutant enzyme P254G
31
24
pyruvate
-
80C, pH 7.5, mutant enzyme I255V
31
25
pyruvate
-
80C, pH 7.5, mutant enzyme I255S
31
28
pyruvate
-
80C, pH 7.5, mutant enzyme T256V
31
31
pyruvate
-
80C, pH 7.5, mutant enzyme T256A
31
38
pyruvate
-
80C, pH 7.5, mutant enzyme T256S
31
41
pyruvate
-
80C, pH 7.5, mutant enzyme I255M
31
145.5
pyruvate
-
80C, pH 7.5, recombinant enzyme
31
204
pyruvate
-
80C, pH 7.5, natural enzyme
31
234.8
pyruvate
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
pH 8.6, 37C
31
3.6
2-oxobutyrate
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
pH 8.6, 37C
371
additional information
additional information
-
pH 8.0, 80C, kinetic parameters for the native and mutant forms of Pyrococcus furiosus ferredoxin
0
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11
nitrite
-
pH 8.4, 80C
10
Sodium nitrite
P80521 and P80522 and P80523 and P80524
37C, pH 7.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
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
0.3
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
pH 8.6, 37C, substrate: indol-3-pyruvate
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
3.6
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
pH 8.6, 37C, substrate: 2-oxobutyrate
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
6.5
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
pH 8.6, 37C, substrate: oxaloacetate
7.4
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
pH 8.6, 37C, substrate: pyruvate
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
20.2
W8CQR1 and W8CQB2 and W8CQB1 and W8CR61
purified enzyme, pH 8.4, 80C
40
-
pH 7.5, 25C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 7.5
-
recombinant enzyme, in 25 mM potassium phosphate
7
P80521 and P80522 and P80523 and P80524
-
7.3
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
at 37 C, maximal activity is obtained at pH 7.3
8
Q9YA13 and Q9YA11
enzyme Ape2126/2128
8.6
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
assay at
9.5
W8CQR1 and W8CQB2 and W8CQB1 and W8CR61
-
pH RANGE
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
assay at
59
P80521 and P80522 and P80523 and P80524
-
60
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
at pH 7.3, the temperature optimum is 60C
80
Q9YA13 and Q9YA11
assay at
95
W8CQR1 and W8CQB2 and W8CQB1 and W8CR61
above
105
Q9YA13 and Q9YA11
enzyme Ape2126/2128
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37 - 60
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
the activity detected at 60C is five times the activity detected at 37C
43 - 71
P80521 and P80522 and P80523 and P80524
43C: about 55% of maximal activity, 71C: about 5% of maximal activity
80 - 110
Q9YA13 and Q9YA11
80C: 45% of maximal activity, 110C: 95% of maximal activity, enzyme Ape2126/2128
LOCALIZATION
ORGANISM
UNIPROT
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
-
electrophoresis on non-denaturing gels
288442
110000
Q9YA13 and Q9YA11
gel filtration, enzyme Ape2126/2128
673610
120000
-
gel filtration
288449
125000
-
polyacrylamide gradient gel electrophoresis
288449
130000
P80521 and P80522 and P80523 and P80524
gel filtration
288448
135000
-
gel filtration
721444
190000
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
-
654391
235000
-
recombinant enzyme, native PAGE
726231
258000
W8CQR1 and W8CQB2 and W8CQB1 and W8CR61
gel filtration
726840
280000
-
dimer, non-denaturing gradient gel in absence of reducing agent
288446
545000
-
tetramer, non-denaturing gradient gel in absence of reducing agent
288446
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
Q24982
x * 140000, SDS-PAGE
?
-
x * 120000, pyruvate : ferredoxin oxidoreductase A, SDS-PAGE
?
-
x * 144000, SDS-PAGE
?
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
the low molecular weight enzyme contains five polypeptides: 47000 Da (alpha), 33000 Da (beta), 25000 (gamma) and 13000 Da (gamma). The subunit stoichiometry for the alpha:beta:gamma:delta subunits is 1:1.08:0.90:1.32. In addition it contains a fifth polypeptide (21500 Da)
?
P80521 and P80522 and P80523 and P80524
x * 48000 + x * 30000 + x * 25000 + x * 15000, SDS-PAGE
?
Methanococcus maripaludis DSMZ 2067
-
the low molecular weight enzyme contains five polypeptides: 47000 Da (alpha), 33000 Da (beta), 25000 (gamma) and 13000 Da (gamma). The subunit stoichiometry for the alpha:beta:gamma:delta subunits is 1:1.08:0.90:1.32. In addition it contains a fifth polypeptide (21500 Da)
-
?
Giardia intestinalis WB
-
x * 140000, SDS-PAGE
-
?
Methanosarcina barkeri DSM 804
-
x * 48000 + x * 30000 + x * 25000 + x * 15000, SDS-PAGE
-
?
Chlamydomonas reinhardtii CC124
-
x * 144000, 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
octamer
W8CQR1 and W8CQB2 and W8CQB1 and W8CR61
2 * 12000 + 2 * 26000 + 2 * 35000 + 2 * 46000, SDS-PAGE
octamer
-
2 * 12000 + 2 * 26000 + 2 * 35000 + 2 * 46000, SDS-PAGE
-
tetramer
-
1 * 46000 + 1 * 31500 + 1 * 29000 + 1 * 24500, SDS-PAGE
tetramer
-
1 * 45000 + 1 * 33000 + 1 * 25000 + 1 * 13000, 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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
-
1 h, stable
288446
70
-
8 h, anoxic conditions, 50% loss of activity
721444
75
-
30 min, anoxic conditions, more than 80% residual activity after heating
721444
80
-
50% loss of activity after 23 min
288442
80
Q9YA13 and Q9YA11
20 min, stable, enzyme Ape2126/2128
673610
85
-
the recombinantly expressed, purified and reconstituted delta subunit is stable for 2 h
721579
90
-
50% loss of activity after 18 min
288442
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
288449
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
following dialysis, the enzyme is very unstable in the absence of glycerol or ethylene glycol, thiamine diphosphate and MgCl2 also help to maintain activity
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
the enzyme is extremely oxygen sensitive, losing 90% of its activity upon exposure to air for 1 h at 0C
P80521 and P80522 and P80523 and P80524
purified enzyme, stored for one year under liquid N2, no loss of activity if thawed anaerobically
-
OXIDATION STABILITY
ORGANISM
UNIPROT
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
the enzyme is very sensitive to O2. Following incubation in air at 2C for 40 min, about 60% of enzyme activity is lost. The half-life is 5.2 min when the purified enzyme is exposed to air in an ice bath. After inactivation of the purified enzyme by oxygen, activity is not restored byreplacing the oxygen with nitrogen and adding 0.01 mM dithionite no activity is lost after dialysis of extract in a basic buffer containing 20 mM potassium Tricine, pH 8.6, 5 mM MgCl2, 0.5 mM dithiothreitol, 0.1 mM thiamine diphosphate, and 10% glycerol
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
654391
oxygen-sensitive enzyme, the t1/2 for the enzyme activity in 50 mM Tris-HCl, pH 7.8 containing 2 mM sodium dithionite and 2 mM DTT is approximately 30 min
W8CQR1 and W8CQB2 and W8CQB1 and W8CR61
726840
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, anaerobically in presence of CoASH, thiamine diphosphate anfd Mg2+, enzyme concentration below 0.02 mg/ml, stable for months
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-20C, 3 weeks, anaerobic conditions, no loss of activity of the partially purified enzyme
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
2C, 2 weeks, anaerobic conditions, no loss of activity
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
-20C, under N2, after addition of 20% (v/v) glycerol to each fraction, the enzyme activity remains nearly constant for several weeks
P80521 and P80522 and P80523 and P80524
4C, storage results in a loss of 80% of the activity within 8 days
P80521 and P80522 and P80523 and P80524
Purification/COMMENTARY
ORGANISM
UNIPROT
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
-
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
-
P80521 and P80522 and P80523 and P80524
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
-
-
W8CQR1 and W8CQB2 and W8CQB1 and W8CR61
Ni-NTA column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
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
LITERATURE
metronidazole-resistant Giardia line 106-2ID10 has decreased PFOR activity
-
APPLICATION
ORGANISM
UNIPROT
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
-