Information on EC 1.2.7.1 - pyruvate synthase

Word Map on EC 1.2.7.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY hide
1.2.7.1
-
RECOMMENDED NAME
GeneOntology No.
pyruvate synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
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
Biosynthesis of antibiotics
-
-
Butanoate metabolism
-
-
Carbon fixation pathways in prokaryotes
-
-
Citrate cycle (TCA cycle)
-
-
Entner-Doudoroff pathway II (non-phosphorylative)
-
-
gluconeogenesis II (Methanobacterium thermoautotrophicum)
-
-
Glycolysis / Gluconeogenesis
-
-
incomplete reductive TCA cycle
-
-
isopropanol biosynthesis (engineered)
-
-
L-glutamate degradation VII (to butanoate)
-
-
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 (engineered)
-
-
Pyruvate metabolism
-
-
reductive monocarboxylic acid cycle
-
-
reductive TCA cycle I
-
-
reductive TCA cycle II
-
-
acetate fermentation
-
-
purine metabolism
-
-
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 hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q9YA13: alpha-subunit, Q9YA11: beta-subunit
Q9YA13 and Q9YA11
-
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
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
V9NGI4, i.e. subunit PorB, V9NFX1, i.e. subunit PorD, V9NGQ2 i.e. subunit PorG, V9NHA1 i.e. subunit PorA, bifunctional pyruvate decarboxylase and pyruvate ferredoxin oxidoreductase
V9NGI4 and V9NFX1 and V9NGQ2 and V9NHA1
-
Manually annotated by BRENDA team
-
-
-
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
Q5JIJ8 i.e. delta subunit, Q5JIJ7 i.e. alpha subunit, Q5JIJ6 i.e. beta subunit
Q5JIJ8 and Q5JIJ7 and Q5JIJ6
UniProt
Manually annotated by BRENDA team
ferredoxin
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
resistance to metronidazole is associated with enzyme down-regulation
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
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
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
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
-
-
?
indol-3 pyruvate + CoA + 2 oxidized methyl viologen
?
show the reaction diagram
oxaloacetate + CoA + oxidized methyl viologen
?
show the reaction diagram
oxaloacetate + CoA + oxidized methyl viologen
? + reduced methyl viologen + H+
show the reaction diagram
pyruvate + CoA + 2 oxidized benzyl viologen
acetyl-CoA + CO2 + 2 reduced benzyl viologen
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 methyl viologen
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
show the reaction diagram
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
pyruvate + CoA + oxidized benzyl viologen
acetyl-CoA + CO2 + reduced benzyl viologen + H+
show the reaction diagram
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
show the reaction diagram
pyruvate + CoA + oxidized ferredoxin 1
acetyl-CoA + CO2 + reduced ferredoxin 1 + H+
show the reaction diagram
pyruvate + CoA + oxidized ferredoxin 2
acetyl-CoA + CO2 + reduced ferredoxin 2 + H+
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 + H+
show the reaction diagram
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
-
-
-
-
?
additional information
?
-
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
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
show the reaction diagram
pyruvate + CoA + oxidized ferredoxin 1
acetyl-CoA + CO2 + reduced ferredoxin 1 + H+
show the reaction diagram
pyruvate + CoA + oxidized ferredoxin 2
acetyl-CoA + CO2 + reduced ferredoxin 2 + H+
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
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
Ferredoxin
-
ferredoxin contains eight atoms of iron and eight acid-labile sulfur groups per molecule. The molecular mass is 6400 Da, the isoelelctric point 3.4. Ferredoxin is stable for at least 1 h at 70C
-
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
thiamine diphosphate
[4Fe-4S]-center
additional information
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
the enzyme is not coenzyme F420-dependent
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4Fe-4S cluster
-
the enzyme contains three [4Fe-4S]2+/1+ clusters all with very low reduction potentials
copper
-
protein contains a copper-center
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 hide
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%
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
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
thiamine diphosphate
-
stimulatory
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 hide
LITERATURE
IMAGE
0.205
2-oxobutyrate
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
pH 8.6, 37C
0.0052 - 0.67
CoA
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 - 0.094
oxidized ferredoxin
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
-
0.14 - 2.33
oxidized methyl viologen
0.07 - 14.5
pyruvate
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 hide
LITERATURE
IMAGE
13
2-oxobutyrate
Methanococcus maripaludis
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
pH 8.6, 37C
18
oxaloacetate
Methanococcus maripaludis
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
pH 8.6, 37C
27
pyruvate
Methanococcus maripaludis
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
pH 8.6, 37C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.6
2-oxobutyrate
Methanococcus maripaludis
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
pH 8.6, 37C
371
68.2
oxaloacetate
Methanococcus maripaludis
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
pH 8.6, 37C
57
7.2 - 234.8
pyruvate
31
additional information
additional information
Pyrococcus furiosus
-
pH 8.0, 80C, kinetic parameters for the native and mutant forms of Pyrococcus furiosus ferredoxin
2
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11
nitrite
-
pH 8.4, 80C
10 - 54
Sodium nitrite
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
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
78
Q56317 and 05650 and Q56316 and O05651
pH 8.4, 80C
119
V9NGI4 and V9NFX1 and V9NGQ2 and V9NHA1
pH 8.4, 80C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
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
8.6
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 hide
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 hide
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
95
W8CQR1 and W8CQB2 and W8CQB1 and W8CR61
above
105
Q9YA13 and Q9YA11
enzyme Ape2126/2128
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
GeneOntology No.
LITERATURE
SOURCE
-
about 1% of activity detected in cytosol
Manually annotated by BRENDA team
-
80% of activity detected in hydrogenosome
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8900
D3DJK0 and D3DJJ8
2 * 21300, subunit PorG, 2 * 44300, subunit PorA, 2 * 32300, subunit PoB, 2 * 26100, subunit PorG, 2 * 8900, subunit PorE, calculated and SDS-PAGE
12000
W8CQR1 and W8CQB2 and W8CQB1 and W8CR61
2 * 12000 + 2 * 26000 + 2 * 35000 + 2 * 46000, SDS-PAGE
14000
V9NGI4 and V9NFX1 and V9NGQ2 and V9NHA1
1 * 45000 plus 1 * 35000 plus 1 * 22000 plus 1 * 14000, SDS-PAGE
15000
P80521 and P80522 and P80523 and P80524
x * 48000 + x * 30000 + x * 25000 + x * 15000, SDS-PAGE
21300
D3DJK0 and D3DJJ8
2 * 21300, subunit PorG, 2 * 44300, subunit PorA, 2 * 32300, subunit PoB, 2 * 26100, subunit PorG, 2 * 8900, subunit PorE, calculated and SDS-PAGE
22000
V9NGI4 and V9NFX1 and V9NGQ2 and V9NHA1
1 * 45000 plus 1 * 35000 plus 1 * 22000 plus 1 * 14000, SDS-PAGE
24000
-
1 * 45000 + 1 * 31000 + 1 * 24000, SDS-PAGE
24500
-
1 * 46000 + 1 * 31500 + 1 * 29000 + 1 * 24500, SDS-PAGE
26000
W8CQR1 and W8CQB2 and W8CQB1 and W8CR61
2 * 12000 + 2 * 26000 + 2 * 35000 + 2 * 46000, SDS-PAGE
26100
D3DJK0 and D3DJJ8
2 * 21300, subunit PorG, 2 * 44300, subunit PorA, 2 * 32300, subunit PoB, 2 * 26100, subunit PorG, 2 * 8900, subunit PorE, calculated and SDS-PAGE
29000
-
1 * 46000 + 1 * 31500 + 1 * 29000 + 1 * 24500, SDS-PAGE
30000
P80521 and P80522 and P80523 and P80524
x * 48000 + x * 30000 + x * 25000 + x * 15000, SDS-PAGE
31000
-
1 * 45000 + 1 * 31000 + 1 * 24000, SDS-PAGE
31500
-
1 * 46000 + 1 * 31500 + 1 * 29000 + 1 * 24500, SDS-PAGE
32300
D3DJK0 and D3DJJ8
2 * 21300, subunit PorG, 2 * 44300, subunit PorA, 2 * 32300, subunit PoB, 2 * 26100, subunit PorG, 2 * 8900, subunit PorE, calculated and SDS-PAGE
33000
-
1 * 45000 + 1 * 33000 + 1 * 25000 + 1 * 13000, SDS-PAGE
34000
-
x * 43000, plus x * 34000, plus x * 23000, plus x * 13000, SDS-PAGE
34936
Q9YA13 and Q9YA11
1 * 71639 + 1 * 34936, calculated from sequence, enzyme Ape2126/2128
43000
-
x * 43000, plus x * 34000, plus x * 23000, plus x * 13000, SDS-PAGE
44300
D3DJK0 and D3DJJ8
2 * 21300, subunit PorG, 2 * 44300, subunit PorA, 2 * 32300, subunit PoB, 2 * 26100, subunit PorG, 2 * 8900, subunit PorE, calculated and SDS-PAGE
48000
P80521 and P80522 and P80523 and P80524
x * 48000 + x * 30000 + x * 25000 + x * 15000, SDS-PAGE
71639
Q9YA13 and Q9YA11
1 * 71639 + 1 * 34936, calculated from sequence, enzyme Ape2126/2128
72000
Q9YA13 and Q9YA11
1 * 72000 + 1 * 35000, SDS-PAGE, enzyme Ape2126/2128
100000
-
electrophoresis on non-denaturing gels
110000
Q9YA13 and Q9YA11
gel filtration, enzyme Ape2126/2128
120000
125000
-
polyacrylamide gradient gel electrophoresis
130000
135000
-
gel filtration
140000
x * 140000, SDS-PAGE
144000
-
x * 144000, SDS-PAGE
155000
-
gel fitlration
156000
Q56317 and 05650 and Q56316 and O05651
gel filtration
157000
V9NGI4 and V9NFX1 and V9NGQ2 and V9NHA1
gel filtration
190000
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
-
235000
-
recombinant enzyme, native PAGE
258000
W8CQR1 and W8CQB2 and W8CQB1 and W8CR61
gel filtration
265000
D3DJK0 and D3DJJ8
gel filtration
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
COMMENTARY hide
LITERATURE
decamer
heterodimer
Q9YA13 and Q9YA11
1 * 71639 + 1 * 34936, calculated from sequence, enzyme Ape2126/2128; 1 * 72000 + 1 * 35000, SDS-PAGE, enzyme Ape2126/2128
homodimer
multimer
-
x * 43000, plus x * 34000, plus x * 23000, plus x * 13000, SDS-PAGE
octamer
tetramer
trimer
-
1 * 45000 + 1 * 31000 + 1 * 24000, SDS-PAGE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
determination of reduction midpoint potentials from 10 to 85C. The enzyme exhibits two voltammetric waves with peaks at -280 and -403 mV at room temperature, indicating multiple redox centers, and a single wave at -420 mV at 85C. Ferredoxin displays a single linear temperature-dependent voltammetric wave at -280 mV at room temperature and -327 mV at 85C
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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
85
-
the recombinantly expressed, purified and reconstituted delta subunit is stable for 2 h
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
purified enzyme, stored for one year under liquid N2, no loss of activity if thawed anaerobically
-
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
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
25C, half-life in presence of air 70 min
-
735659
both pyruvate decarboxylase and pyruvate ferredoxin oxidoreductase activity are extremely oxygen sensitive, 50% loss of activity upon exposure to air at room temperature within 15 min
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
the enzyme is efficiently protected when cells are exposed to air or H2O2
-
725463
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
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
-
288436
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
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 3 weeks, anaerobic conditions, no loss of activity of the partially purified enzyme
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
-70C, anaerobically in presence of CoASH, thiamine diphosphate anfd Mg2+, enzyme concentration below 0.02 mg/ml, stable for months
-
2C, 2 weeks, anaerobic conditions, no loss of activity
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
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
DE52 column chromatography, DEAE-cellulose column chromatography, and Sephadex G25 gel filtration
-
enzyme Ape2126/2128
Q9YA13 and Q9YA11
Ni-NTA column chromatography
nickel affinity column chromatography
-
purification under strictly unaerobic conditions
-
purified enzyme shos a brownish colour characteristic of iron-sulfur containing proteins
Q56317 and 05650 and Q56316 and O05651
purified enzyme shows a brownish colour characteristic of iron-sulfur containing proteins
V9NGI4 and V9NFX1 and V9NGQ2 and V9NHA1
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
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
D3DJK0 and D3DJJ8
expression in Escherichia coli, enzyme Ape2126/2128
Q9YA13 and Q9YA11
the gene encoding the delta-subunit is expressed in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
metronidazole-resistant Giardia line 106-2ID10 has decreased PFOR activity
-
the operon organization for Pyrococcus furiosus pyruvate ferredoxin oxidoreductase POR and 2-oxoisovalerate ferredoxin oxidoreductase VOR is porG-vorDAB-porDAB, wherein the gamma subunit is shared by the two enzymes
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
synthesis
-
engineering of Thermoanaerobacterium saccharolyticum to produce ethanol at high yield. Knockout of genes involved in organic acid formation (acetate kinase, phosphate acetyltransferase, and L-lactate dehydrogenase) results in a strain able to produce ethanol as the only detectable organic product and substantial changes in electron flow relative to the wild type. Ethanol formation in the engineered strain ALK2 utilizes pyruvate:ferredoxin oxidoreductase with electrons transferred from ferredoxin to NAD(P). The homoethanologenic phenotype is stable for more than 150 generations in continuous culture. The growth rate of strain ALK2 is similar to the wild-type strain, with a reduction in cell yield proportional to the decreased ATP availability resulting from acetate kinase inactivation. Glucose and xylose are coutilized and utilization of mannose and arabinose commences before glucose and xylose are exhausted. Using strain ALK2 in simultaneous hydrolysis and fermentation experiments at 50C allows a 2.5fold reduction in cellulase loading compared with using Saccharomyces cerevisiae at 37C. The maximum ethanol titer produced by strain ALK2 is 37 g/liter
Show AA Sequence (2118 entries)
Please use the Sequence Search for a specific query.