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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

Reaction

pyruvate
+
CoA
 +
oxidized ferredoxin
=
acetyl-CoA
 +
CO2
 +
reduced ferredoxin
 + 2 H+

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

     1 Oxidoreductases
         1.2 Acting on the aldehyde or oxo group of donors
             1.2.7 With an iron-sulfur protein as acceptor
                1.2.7.1 pyruvate synthase

Inhibitors

Inhibitors on EC 1.2.7.1 - pyruvate synthase

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INHIBITOR
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 25°C. Attempts to reactivate the enzyme by anoxic incubation in the presence of 2 mM dithiothreitol fail
Dithionite
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
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
nitazoxanide
-
52% inhibition at 0.040 mM, 25°C, pH 7.4
Sodium nitrite
thiamin diphosphate
CoA binds to domain III and CoA binding and domain III movement drive electron transfer from the TPP, which is coordinated by domains I and IV, into the domain V [4Fe-4S] clusters
VPC161183
-
36% inhibition at 0.040 mM, 25°C, pH 7.4
VPC161195
-
56% inhibition at 0.040 mM, 25°C, pH 7.4
VPC161219
-
61% inhibition at 0.040 mM, 25°C, pH 7.4
VPC162125
-
71% inhibition at 0.040 mM, 25°C, pH 7.4
VPC162134
-
75% inhibition at 0.040 mM, 25°C, pH 7.4
VPC16a1011
-
34% inhibition at 0.040 mM, 25°C, pH 7.4
VPC16b1094
-
66% inhibition at 0.040 mM, 25°C, pH 7.4
VPC16b2031
-
84% inhibition at 0.040 mM, 25°C, pH 7.4
[4Fe-4S]-center
CoA binds to domain III and CoA binding and domain III movement drive electron transfer from the TPP, which is coordinated by domains I and IV, into the domain V [4Fe-4S] clusters
additional information
-