1.2.7.1: pyruvate synthase
This is an abbreviated version!
For detailed information about pyruvate synthase, go to the full flat file.
Word Map on EC 1.2.7.1
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1.2.7.1
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ferredoxins
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acetyl-coa
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clostridium
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hydrogenase
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metronidazole
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hydrogenosomal
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trichomonas
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vaginalis
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thiamin
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histolytica
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entamoeba
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giardia
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desulfovibrio
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pasteurianum
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low-potential
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duodenalis
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trichomoniasis
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2-oxoacids
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flavodoxins
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adp-forming
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nitazoxanide
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formate-lyase
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wood-ljungdahl
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2-oxoacid:ferredoxin
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5-nitroimidazole
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acetogenic
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metronidazole-resistant
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africanus
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tritrichomonas
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hydrogen-producing
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foramen
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amitochondriate
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synthesis
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ferredoxin-type
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indolepyruvate
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biofuel production
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analysis
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biotechnology
- 1.2.7.1
- ferredoxins
- acetyl-coa
- clostridium
- hydrogenase
- metronidazole
- hydrogenosomal
- trichomonas
- vaginalis
- thiamin
- histolytica
- entamoeba
- giardia
- desulfovibrio
- pasteurianum
-
low-potential
- duodenalis
-
trichomoniasis
- 2-oxoacids
- flavodoxins
-
adp-forming
- nitazoxanide
- formate-lyase
-
wood-ljungdahl
-
2-oxoacid:ferredoxin
-
5-nitroimidazole
-
acetogenic
-
metronidazole-resistant
- africanus
-
tritrichomonas
-
hydrogen-producing
-
foramen
-
amitochondriate
- synthesis
-
ferredoxin-type
- indolepyruvate
- biofuel production
- analysis
- biotechnology
Reaction
Synonyms
2-ketobutyrate synthase, 2-oxobutyrate (methylviologen), 2-oxobutyrate synthase (benzylviologen), 2-oxobutyrate-ferredoxin oxidoreductase, alpha-ketobutyrate synthase, alpha-ketobutyrate-ferredoxin oxidoreductase, AP120, Ape2126/2128, bifunctional pyruvate decarboxylase/pyruvate ferredoxin oxidoreductase, EC 1.2.7.2, Moth_0064, NifJ1, OFOR, PFO, PFO A, PFOR, Pfor1, PforA, PFR, PFR1, POR, PorEDABG, pyruvate ferredoxin oxidoreductase, pyruvate-ferredoxin oxidoreductase, pyruvate:Fd oxidoreductase, pyruvate:ferredoxin oxidoreductase, pyruvate:ferredoxin oxidoreductase A, synthase, 2-oxobutyrate, TKV_c04340, Tsac_0046, TTE0445
ECTree
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Cofactor
Cofactor on EC 1.2.7.1 - pyruvate synthase
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FAD
it is possible that flavins play an important regulatory or structural role in the enzyme
Ferredoxin
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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 70°C
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FMN
it is possible that flavins play an important regulatory or structural role in the enzyme
pyruvate ferredoxin oxidoreductase activity is strictly CoA-dependent, desulfo-CoA does not serve as cofactor
CoA
pyruvate ferredoxin oxidoreductase activity is strictly CoA-dependent, desulfo-CoA does not serve as cofactor. The pyruvate decarboxylase activity accepts desulfo-CoA
thiamine diphosphate
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essential cofactor, upon addition of Mg2+, an ion that stabilizes thiamine diphosphate, the enzymatic activity almost doubles
thiamine diphosphate
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per mol, the enzyme contains 0.8 mol thiamine diphosphate
thiamine diphosphate
contains 1 mol thiamine diphosphate per mol of enzyme
thiamine diphosphate
the beta subunit contains four conserved cysteines in addition to a thiamine diphosphate-binding domain
thiamine diphosphate
the beta subunit contains four conserved cysteines in addition to a thiamine diphosphate-binding domain
thiamine diphosphate
the enzyme contained 1 mol/mol thiamine diphosphate
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the enzyme contains at least two [4Fe-4S] clusters. The purified and reconstituted delta subunit contains 8 Fe mol/mol
[4Fe-4S]-center
enzyme contains an extremely thermostable [4Fe-4S] ferredoxin. The Fe-S cluster has three cysteines and one aspartate as the cluster ligands. The 4Fe ferredoxin is degraded to 3Fe ferredoxin during aerobic purification. The aerobically-purified ferredoxin is reversibly converted back to the [4Fe-4S] ferredoxin by the addition of ferrous ions under reducing conditions. The anaerobically-purified [4Fe-4S] ferredoxin is quite stable, little degradtion is observed over 20 h at 100°C, while the half-life of the aerobically-purified ferredoxin is 10 h at 100°C
[4Fe-4S]-center
protein contains at least two [4Fe-4S] ferredoxin-type clusters
[4Fe-4S]-center
protein contains at least two [4Fe-4S] ferredoxin-type clusters
[4Fe-4S]-center
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proteins contains at least two ferredoxin-type [4Fe-4S] clusters per molecule. Km value for ferredoxin is 0.026 microM
[4Fe-4S]-center
the delta subunit contains two ferredoxin-type [4Fe-4S] cluster binding motifs, CXXCXXCXXXCP
[4Fe-4S]-center
the delta subunit contains two ferredoxin-type [4Fe-4S] cluster binding motifs, CXXCXXCXXXCP
the enzyme is not coenzyme F420-dependent
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additional information
FAD, FMN and lipoic acid are not found
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