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2-hydroxyethylidene-thiamine diphosphate + 2,6-dichlorophenolindophenol
S-acetyldihydrolipoamide + reduced 2,6-dichlorophenolindophenol
-
-
-
?
2-oxobutanoate + oxidized 2,6-dichlorophenolindophenol
propanal + CO2 + reduced 2,6-dichlorophenolindophenol
-
-
-
?
2-oxoisovalerate + oxidized 2,6-dichlorophenolindophenol
2-methylpropanal + CO2 + reduced 2,6-dichlorophenolindophenol
16% of the activity with 2-oxobutanoate
-
-
?
2-oxovalerate + oxidized 2,6-dichlorophenolindophenol
butanal + CO2 + reduced 2,6-dichlorophenolindophenol
49% of the activity with 2-oxobutanoate
-
-
?
acetaldehyde + benzaldehyde
(R)-phenylacetylcarbinol
alpha-ketobutyrate + Fe(CN)63- + H2O
hydroxyacetate + CO2 + Fe(CN)64-
-
-
-
?
alpha-ketobutyrate + lipoamide
S-propionyldihydrolipoamide + CO2
-
-
-
?
pyruvate + CoA + 2,6-dichlorophenolindophenol
acetyl-CoA + CO2 + reduced 2,6-dichlorophenolindophenol
-
-
-
?
pyruvate + CoA + ferricyanide
acetyl-CoA + CO2 + ferrocyanide
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
pyruvate + CoA + oxidized 2,6-dichlorophenolindophenol
acetyl-CoA + CO2 + reduced 2,6-dichlorophenolindophenol
pyruvate + E2p lipoyl domain
acetylated E2p lipoyl domain + CO2
-
-
-
-
?
pyruvate + Fe(CN)63- + H2O
CO2 + Fe(CN)64-
-
-
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
pyruvate + lipoyl domain
acetylated lipoyl domain + CO2
-
-
-
-
r
pyruvate + oxidized 2,6-dichlorophenolindophenol
acetaldehyde + CO2 + reduced 2,6-dichlorophenolindophenol
pyruvate + pyruvate dehydrogenase complex subunit E2p
?
-
-
-
-
?
pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine
[dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2
pyruvate + [dihydrolipoyllysine-residue acetyltransferase]-lipoyllysine
[dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2
-
-
-
-
?
additional information
?
-
acetaldehyde + benzaldehyde
(R)-phenylacetylcarbinol
-
-
-
-
?
acetaldehyde + benzaldehyde
(R)-phenylacetylcarbinol
-
-
-
-
?
acetaldehyde + benzaldehyde
(R)-phenylacetylcarbinol
-
-
-
-
?
acetaldehyde + benzaldehyde
(R)-phenylacetylcarbinol
-
-
-
-
?
acetaldehyde + benzaldehyde
(R)-phenylacetylcarbinol
-
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
enzyme E1 is a component of the pyruvate dehydrogenase multienzyme complex PDHc, and catalyzes the first step of the multistep process
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
reaction of the citric acid or Krebs cycle
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
-
ir
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
first step of the overall reaction of the pyruvate dehydrogenase complex
-
-
ir
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
ir
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
enzyme is the E1alpha component of the pyruvate dehydrogenase multienzyme complex, regulation via reversible phosphorylation, age-related in crease in enzyme E1alpha activity due to age-related decline in pyruvate dehydrogenase kinase PDK-4, overview
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
-
?
pyruvate + CoA + oxidized 2,6-dichlorophenolindophenol
acetyl-CoA + CO2 + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
pyruvate + CoA + oxidized 2,6-dichlorophenolindophenol
acetyl-CoA + CO2 + reduced 2,6-dichlorophenolindophenol
-
-
-
?
pyruvate + CoA + oxidized 2,6-dichlorophenolindophenol
acetyl-CoA + CO2 + reduced 2,6-dichlorophenolindophenol
-
artificial electron acceptor
-
-
?
pyruvate + CoA + oxidized 2,6-dichlorophenolindophenol
acetyl-CoA + CO2 + reduced 2,6-dichlorophenolindophenol
-
artifical electron acceptor
-
-
ir
pyruvate + CoA + oxidized 2,6-dichlorophenolindophenol
acetyl-CoA + CO2 + reduced 2,6-dichlorophenolindophenol
-
-
-
?
pyruvate + CoA + oxidized 2,6-dichlorophenolindophenol
acetyl-CoA + CO2 + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
-
additional reactions of complex, e. g. reduction of K3Fe(CN)6
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
-
specific for
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
-
-
-
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
-
-
-
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
-
in overall reaction of pyruvate dehydrogenase complex, pyruvate can be replaced by 2-ketobutyrate
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
-
additional reactions of complex, e. g. reduction of K3Fe(CN)6
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
Hansenula sp.
-
additional reactions of complex, e. g. reduction of K3Fe(CN)6
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
-
-
-
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
-
-
-
ir
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
-
in overall reaction of pyruvate dehydrogenase complex, pyruvate can be replaced by hydroxypyruvate
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
-
in overall reaction of pyruvate dehydrogenase complex, pyruvate can be replaced by 2-ketobutyrate
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
-
low reactivity with 2-ketovalerate
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
-
low reactivity with 2-ketoisovalerate
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
-
low reactivity with 2-ketoisocaproate
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
-
-
-
?
pyruvate + oxidized 2,6-dichlorophenolindophenol
acetaldehyde + CO2 + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
pyruvate + oxidized 2,6-dichlorophenolindophenol
acetaldehyde + CO2 + reduced 2,6-dichlorophenolindophenol
17% of the activity with 2-oxobutanoate
-
-
?
pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine
[dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2
-
-
-
-
?
pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine
[dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2
-
-
-
?
additional information
?
-
-
conjugates of indole-3-acetic acid with amino acids act as hormones and e.g. inhibit root elongation, the sensitivity of the mutant iar4-1 plant against these conjugates and plant hormones is reduced compared to the wild-type, overview
-
-
?
additional information
?
-
non-complex-bound E1p shows the same cooperativity as found for complex-bound E1p in the pyruvate dehydrogenase complex, EC 1.2.1.104. A Hill coefficient of 1.2-1.6 is calculated for non-complex bound E1p
-
-
-
additional information
?
-
-
enzyme is essential for the tricatrboxylic cycle
-
-
?
additional information
?
-
-
overall reaction of the multienzyme complex, overview
-
-
?
additional information
?
-
-
N-terminal residues 1-45 of the pyruvate dehydrogenase complex E1 subunit interact with the E2 subunit and are required for activity of the complex but not for reductive acetylation of the E2 subunit
-
-
?
additional information
?
-
reactions performed by the whole enzyme complex, overview
-
-
?
additional information
?
-
-
reactions performed by the whole enzyme complex, overview
-
-
?
additional information
?
-
-
binds to the di-domain (lipoyl domain + linker + peripheral subunit binding domain) of the dihydrolipoyl acetyltransferase (E2) component for acetylation
-
-
?
additional information
?
-
-
determination of free short-chain CoA esters in rat heart
-
-
?
additional information
?
-
-
regulatory role of pirin in the process of pyruvate catabolism through interaction with enzyme and inhibition of pyruvate dehydrogenase complex
-
-
?
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(2-chlorophenyl)(dimethoxyphosphoryl)methyl [3-(trifluoromethyl)phenoxy]acetate
-
(3,4-dichlorophenyl)(dimethoxyphosphoryl)methyl [3-(trifluoromethyl)phenoxy]acetate
-
(3-chlorophenyl)(dimethoxyphosphoryl)methyl [3-(trifluoromethyl)phenoxy]acetate
-
(4-chlorophenyl)(dimethoxyphosphoryl)methyl [3-(trifluoromethyl)phenoxy]acetate
-
(dimethoxyphosphoryl)(4-methylphenyl)methyl [3-(trifluoromethyl)phenoxy]acetate
-
(dimethoxyphosphoryl)(phenyl)methyl (2,3-dichlorophenoxy)acetate
-
(dimethoxyphosphoryl)(phenyl)methyl (2,6-dichlorophenoxy)acetate
-
(dimethoxyphosphoryl)(phenyl)methyl (2-chloro-5-methylphenoxy)acetate
-
(dimethoxyphosphoryl)(phenyl)methyl (3-fluorophenoxy)acetate
-
(dimethoxyphosphoryl)(phenyl)methyl (4-chloro-2-methylphenoxy)acetate
-
(dimethoxyphosphoryl)(phenyl)methyl (4-chloro-3-methylphenoxy)acetate
-
(dimethoxyphosphoryl)(phenyl)methyl (4-chlorophenoxy)acetate
-
(dimethoxyphosphoryl)(phenyl)methyl (4-fluorophenoxy)acetate
-
1-(dimethoxyphosphoryl)ethyl (2,3-dichlorophenoxy)acetate
-
1-(dimethoxyphosphoryl)ethyl (2,6-dichlorophenoxy)acetate
-
1-(dimethoxyphosphoryl)ethyl (2-chloro-5-methylphenoxy)acetate
-
1-(dimethoxyphosphoryl)ethyl (3-fluorophenoxy)acetate
-
1-(dimethoxyphosphoryl)ethyl (4-chloro-2-methylphenoxy)acetate
-
1-(dimethoxyphosphoryl)ethyl (4-chloro-3-methylphenoxy)acetate
-
1-(dimethoxyphosphoryl)ethyl (4-chlorophenoxy)acetate
-
1-(dimethoxyphosphoryl)ethyl (4-fluorophenoxy)acetate
-
2,2'-Dithiopyridine
-
1.1 mM, 30% inhibition
2,2,2-trichloro-1-(dimethoxyphosphoryl)ethyl (2,3-dichlorophenoxy)acetate
-
2,2,2-trichloro-1-(dimethoxyphosphoryl)ethyl (2-chloro-5-methylphenoxy)acetate
-
2,2,2-trichloro-1-(dimethoxyphosphoryl)ethyl (3-fluorophenoxy)acetate
-
2,2,2-trichloro-1-(dimethoxyphosphoryl)ethyl (4-chloro-2-methylphenoxy)acetate
-
2,2,2-trichloro-1-(dimethoxyphosphoryl)ethyl (4-chloro-3-methylphenoxy)acetate
-
2,2,2-trichloro-1-(dimethoxyphosphoryl)ethyl (4-chlorophenoxy)acetate
-
2,2,2-trichloro-1-(dimethoxyphosphoryl)ethyl (4-fluorophenoxy)acetate
-
3-Bromopyruvate
-
suicide substrate
3-deazathiamine diphosphate
4-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-5-iodo-1H-1,2,3-triazol-4-yl)methoxy)benzonitrile
-
exhibits very good enzyme-selective inhibition of PDH-E1 between pig heart and Escherichia coli and activity against Rhizoctonia solani and Botrytis cinerea even at 12.5 lg/ml
5,5'-dithiobis(2-nitrobenzoate)
-
1.1 mM, 35% inhibition
5-((4-((4-bromophenoxy)methyl)-5-iodo-1H-1,2,3-triazol-1-yl)methyl)-2-methylpyrimidin-4-amine
-
exhibits activity against Rhizoctonia solani and Botrytis cinerea even at 12.5 lg/ml
5-((4-((4-chloro-3-methylphenoxy)methyl)-5-iodo-1H-1,2,3-triazol-1-yl)methyl)-2-methylpyrimidin-4-amine
-
-
5-((4-((4-chlorophenoxy)methyl)-5-iodo-1H-1,2,3-triazol-1-yl)methyl)-2-methylpyrimidin-4-amine
acetyl-CoA
product inhibition, acetyl CoA interacts directly with the E1p component
AgNO3
-
18 mol per mol enzyme, complete inhibition
Aluminium sulfate
-
1.1 mM, 35% inhibition
Ba2+
-
0.11 mM, 10% inhibition
Cd2+
-
0.032 mM, complete inhibition
citrate
-
noncompetitive inhibition
CoA
allosteric inhibition
Cu2+
-
0.36 mM, complete inhibition
CuSO4
EC50 value against Synechocystis sp. PCC 6803 is 0.002 mM
D-glucose
-
treatment of cardiac fibroblasts with 35 mM D-glucose for 72 h reduces the PDH activity remarkably. 0.2 mM thiamine dramatically recovers the high glucose-induced PDH inhibition
EDTA
-
0.036 mM, 40% inhibition, 0.36 mM, complete inhibition, reversed by addition of excess Mg2+ and Ca2+
Fluoropyruvate
-
competitive with respect to pyruvate, both free and complex bound enzyme behave in the same manner
KCl
-
at 2 M, 50% residual activity of enzyme expressed in Escherichia coli
methyl acetylphosphonate
-
phosphonate analogue of pyruvate, leading to formation of a stable 1,4-imino-2-alpha-phosphonolactyl-thiamindiphosphate
Methylacetylphosphonate
-
-
MgATP2-
-
due to phosphorylation of the enzyme by pyruvate dehydrogenase kinase
N-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-1H-1,2,3-triazol-4-yl) methyl)-2,4,6-trimethylbenzenesulfonamide
thiamim diphosphate analogue, EC50 value against Synechocystis sp. PCC 6803 is 0.0043 mM
-
N-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-1H-1,2,3-triazol-4-yl) methyl)-2-nitrobenzenesulfonamide
thiamim diphosphate analogue, EC50 value against Synechocystis sp. PCC 6803 is 0.0063 mM
-
N-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-1H-1,2,3-triazol-4-yl) methyl)-4-bromobenzenesulfonamide
thiamin diphosphate analogue, EC50 value against Synechocystis sp. PCC 6803 is 0.009 mM
-
N-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-5-iodo-1H-1,2,3-triazol-4-yl) methyl)-4-chlorobenzenesulfonamide
thiamim diphosphate analogue, EC50 value against Synechocystis sp. PCC 6803 is 0.0018 mM
-
N-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-5-iodo-1H-1,2,3-triazol-4-yl)methyl)-2,4,6-trimethylbenzenesulfonamide
thiamim diphosphate analogue, EC50 value against Synechocystis sp. PCC 6803 is 0.002 mM
-
N-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-5-iodo-1H-1,2,3-triazol-4-yl)methyl)-4-bromobenzenesulfonamide
thiamim diphosphate analogue, EC50 value against Synechocystis sp. PCC 6803 is 0.002 mM
-
N-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-5-iodo-1H-1,2,3-triazol-4-yl)methyl)-4-fluorobenzenesulfonamide
thiamim diphosphate analogue, EC50 value against Synechocystis sp. PCC 6803 is 0.0017 mM
-
N-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-5-iodo-1H-1,2,3-triazol-4-yl)methyl)-4-methoxybenzenesulfonamide
thiamim diphosphate analogue, EC50 value against Synechocystis sp. PCC 6803 is 0.0027 mM
-
N-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-5-iodo-1H-1,2,3-triazol-4-yl)methyl)-4-methylbenzenesulfonamide
thiamim diphosphate analogue, EC50 value against Synechocystis sp. PCC 6803 is 0.002 mM
-
N-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-5-iodo-1H-1,2,3-triazol-4-yl)methyl)-4-nitrobenzenesulfonamide
thiamim diphosphate analogue, EC50 value against Synechocystis sp. PCC 6803 is 0.0016 mM, EC50 value against Microcystis aeruginosa FACHB905 is 0.0001 mM
-
N-ethylmaleimide
-
1.1 mM, 50% inhibition
NaBH4
-
rapid inactivation in the presence of thiamine diphosphate, may reduce thiamine diphosphate to produce a reversible inhibitor
NaCl
-
at 2 M, 50% residual activity of enzyme expressed in Escherichia coli
O,O-dimethyl (2,3-dichlorophenoxyacetoxy)(furan-2-yl)-methylphosphonate
-
O,O-dimethyl (2,3-dichlorophenoxyacetoxy)(thien-2-yl)-methylphosphonate
-
O,O-dimethyl (2,4-dichlorophenoxyacetoxy)(furan-2-yl)-methylphosphonate
-
O,O-dimethyl (2,4-dichlorophenoxyacetoxy)(thien-2-yl)-methylphosphonate
-
O,O-dimethyl (2,6-dichlorophenoxyacetoxy)(furan-2-yl)-methylphosphonate
-
O,O-dimethyl (2,6-dichlorophenoxyacetoxy)(thien-2-yl)-methylphosphonate
-
O,O-dimethyl (2-chloro-5-methylphenoxyacetoxy)(furan-2-yl)methylphosphonate
-
O,O-dimethyl (2-chloro-5-methylphenoxyacetoxy)(thien-2-yl)methylphosphonate
-
O,O-dimethyl (3-fluorophenoxyacetoxy)(furan-2-yl)methylphosphonate
-
O,O-dimethyl (3-fluorophenoxyacetoxy)(thien-2-yl)methylphosphonate
-
O,O-dimethyl (4-chloro-2-methylphenoxyacetoxy)(furan-2-yl)methylphosphonate
-
O,O-dimethyl (4-chloro-2-methylphenoxyacetoxy)(thien-2-yl)methylphosphonate
-
O,O-dimethyl (4-chloro-3-methylphenoxyacetoxy)(furan-2-yl)methylphosphonate
-
O,O-dimethyl (4-chloro-3-methylphenoxyacetoxy)(thien-2-yl)methylphosphonate
-
O,O-dimethyl (4-chlorophenoxyacetoxy)(furan-2-yl)methylphosphonate
-
O,O-dimethyl (4-chlorophenoxyacetoxy)(thien-2-yl)methylphosphonate
-
O,O-dimethyl (4-fluorophenoxyacetoxy)(furan-2-yl)methylphosphonate
-
p-chloromercuribenzenesulfonate
-
8 mol per mol enzyme, complete inhibition
p-chloromercuribenzoate
-
8 mol per mol enzyme, complete inhibition
pyruvate dehydrogenase kinase
-
phosphorylation of E1p by pyruvate dehydrogenase kinase isoforms inactivates the pyruvate dehydrogenase complex
-
sodium methyl [[[(2,4-dichlorophenoxy)acetyl]oxy](2,4-dichlorophenyl)methyl]phosphonate
-
sodium methyl [[[(2,4-dichlorophenoxy)acetyl]oxy](3-nitrophenyl)methyl]phosphonate
-
sodium methyl [[[(2,4-dichlorophenoxy)acetyl]oxy](4-fluorophenyl)methyl]phosphonate
-
sodium methyl [[[(2,4-dichlorophenoxy)acetyl]oxy](4-methoxyphenyl)methyl]phosphonate
-
sodium methyl [[[(2,4-dichlorophenoxy)acetyl]oxy](phenyl)methyl]phosphonate
-
sodium o-methyl (2,4-dichlorophenoxyacetoxy)(2-chlorophenyl)methylphosphonate
-
sodium o-methyl (2,4-dichlorophenoxyacetoxy)(3,4-dichlorophenyl)methyl phosphonate
-
sodium o-methyl (2,4-dichlorophenoxyacetoxy)(4-chlorophenyl)methylphosphonate
-
sodium o-methyl (2,4-dichlorophenoxyacetoxy)(4-methylphenyl)methylphosphonate
-
sodium o-methyl (2,4-dichlorophenoxyacetoxy)(furan-2-yl)methylphosphonate
-
sodium o-methyl (2,4-dichlorophenoxyacetoxy)(pyridin-2-yl)methylphosphonate
-
Tetrahydrothiamine diphosphate
-
cis-isomer, 0.0013 mM, 50% inhibition
thiamine 2-thiazolone diphosphate
crystallization data of complex with enzyme
thiamine 2-thiothiazolone diphosphate
thiamine thiazolone diphosphate
thiamine thiothiazolone diphosphate
-
-
3-deazathiamine diphosphate
-
competitive inhibitor, compound added to the culture medium for HeLa cells does not hamper the rate of cell growth and shows not significant impact on the viability of the cells
3-deazathiamine diphosphate
-
competitive inhibitor
5-((4-((4-chlorophenoxy)methyl)-5-iodo-1H-1,2,3-triazol-1-yl)methyl)-2-methylpyrimidin-4-amine
-
exhibits activity against Rhizoctonia solani even at 12.5 lg/ml and almost 5.5 times more inhibitory potency against Botryttis cinerea than pyrimethanil
5-((4-((4-chlorophenoxy)methyl)-5-iodo-1H-1,2,3-triazol-1-yl)methyl)-2-methylpyrimidin-4-amine
formation of intermolecular hydrogen bonding and halogen bonding. The 5-iodo-1,2,3-triazole and benzene ring play important roles in the biological activities of the compound. The iodine atom may participate in the halogen bonding with the negatively charged and can form a halogen bonding with the O atom of Asp521 in the active site of PDH-E1
Oxythiamine diphosphate
-
competitive inhibitor, shows a significant cytostatic effect on HeLa cell culture
Oxythiamine diphosphate
-
competitive inhibitor
phosphorylation
-
-
-
phosphorylation
-
phosphorylation inactivates recombinant alpha2,beta2 tetramer in about 10 min
-
thiamine 2-thiothiazolone diphosphate
-
-
thiamine 2-thiothiazolone diphosphate
-
-
thiamine thiazolone diphosphate
inhibits potently the E1 component of the pyruvate dehydrogenase multienzyme complex PDHc, competitive to cofactor thiamine diphosphate, binding structure and determinants, binding induced reorganisation of the active site conformation, mechanism, K392 is important, overview
thiamine thiazolone diphosphate
-
-
additional information
-
effects of several plant hormones and auxin derivatives
-
additional information
-
enzyme from chloroplast is not inhibited by ATP
-
additional information
-
there is no significant change in the PDH activity in the presence of D-mannitol (35 mM)
-
additional information
-
not inhibited by ATP
-
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D15A
-
site-directed mutagenesis, 0.19% remaining activity with NAD+ and 16% reduced E1 activity with 2,6-dichlorophenolindophenol as electron acceptor compared to the wild-type E1
D549A
-
in the mutant, binding and reductive acetylation of E2p lipoyl domains are highly impaired
D7A
-
site-directed mutagenesis, 0.14% remaining activity with NAD+ and 63% reduced E1 activity with 2,6-dichlorophenolindophenol as electron acceptor compared to the wild-type E1
D9A
-
site-directed mutagenesis, inactive with NAD+, 80% reduced E1 activity with 2,6-dichlorophenolindophenol as electron acceptor compared to the wild-type E1
E12D
-
site-directed mutagenesis, 2.3% remaining activity with NAD+ and 90% reduced E1 activity with 2,6-dichlorophenolindophenol as electron acceptor compared to the wild-type E1
E12Q
-
site-directed mutagenesis, 3.3% remaining activity with NAD+ and 59% reduced E1 activity with 2,6-dichlorophenolindophenol as electron acceptor compared to the wild-type E1
E401A
9.56% of overall wild type activity and 23.4% of wild type activity with 2,6-dichloroindolphenol
E410K
-
CC-bond formation is dramatically slowed down (10-fold compared with E1ec) in E401K, the loop dynamics apparently greatly influences covalent addition of substrate to the enzyme-bound thiamine diphosphate
I11A
-
site-directed mutagenesis, 94% remaining activity with NAD+ and E1 activity with 2,6-dichlorophenolindophenol as electron acceptor is like the wild-type E1 activity
K403A
11.6% of overall wild type activity and 98.0% of wild type activity with 2,6-dichloroindolphenol
K403E
0.56% of overall wild type activity and 5.46% of wild type activity with 2,6-dichloroindolphenol
K410A
23.0% of overall wild type activity and 31.6% of wild type activity with 2,6-dichloroindolphenol
K410E
3.7% of overall wild type activity and 26.1% of wild type activity with 2,6-dichloroindolphenol
K411A
68.2% of overall wild type activity and 77.5% of wild type activity with 2,6-dichloroindolphenol
K411E
38.0% of overall wild type activity and 88.0% of wild type activity with 2,6-dichloroindolphenol
N404A
1.81% of overall wild type activity and 45.1% of wild type activity with 2,6-dichloroindolphenol
P10A
-
site-directed mutagenesis, unaltered activity with NAD+ and 50% reduced E1 activity with 2,6-dichlorophenolindophenol as electron acceptor compared to the wild-type E1
Q408A
31.5% of overall wild type activity and 112.1% of wild type activity with 2,6-dichloroindolphenol
R14A
-
site-directed mutagenesis, 0.25% remaining activity with NAD+ as electron acceptor, E1 activity with 2,6-dichlorophenolindophenol is like the wild-type E1 activity
T13A
-
site-directed mutagenesis, 13% remaining activity with NAD+ and 26% reduced E1 activity with 2,6-dichlorophenolindophenol as electron acceptor compared to the wild-type E1
Y177F
-
7% of wild-type activity in enzyme complex
D203A
enzymatic activity similar to wild-type, mutant retains the normal capacity to bind the peripheral subunit-binding domain
D276A
-
site-directed mutagenesis, reduced activity with pyruvate compared to the wild-type enzyme
E251A
enzymatic activity similar to wild-type, mutant retains the normal capacity to bind the peripheral subunit-binding domain
E285A
enzymatic activity similar to wild-type, mutant retains the normal capacity to bind the peripheral subunit-binding domain. Mutant subunit dissociates from the wild-type peripheral subunit-binding domain about 9fold faster than wild-type
F266A
-
site-directed mutagenesis, reduced activity with pyruvate compared to the wild-type enzyme
F324A
enzymatic activity similar to wild-type, mutant retains the normal capacity to bind the peripheral subunit-binding domain. Mutant subunit dissociates from the wild-type peripheral subunit-binding domain about 13fold faster than wild-type
H128A
-
mutation in subunit E1beta, residue His128 provides the proton required to protonate the incoming dithiolane ring in the reductive acetylation of the lipoyl goup
H271A
-
mutation in subunit E1alpha, residue His271 stabilizes the dianion formed during decarboxylation of the 2-oxo acid
K252A
enzymatic activity similar to wild-type, mutant retains the normal capacity to bind the peripheral subunit-binding domain
M322A
enzymatic activity similar to wild-type, mutant retains the normal capacity to bind the peripheral subunit-binding domain
N323A
enzymatic activity similar to wild-type, mutant retains the normal capacity to bind the peripheral subunit-binding domain
R255A
enzymatic activity similar to wild-type, mutant retains the normal capacity to bind the peripheral subunit-binding domain
R267A
-
site-directed mutagenesis, highly reduced activity with pyruvate compared to the wild-type enzyme
R282A
-
site-directed mutagenesis, reduced activity with pyruvate compared to the wild-type enzyme
S283C
-
site-directed mutagenesis, reduced activity with pyruvate compared to the wild-type enzyme
Y281A
-
site-directed mutagenesis, reduced activity with pyruvate compared to the wild-type enzyme
Y281A/R282A
-
site-directed mutagenesis, highly reduced activity with pyruvate compared to the wild-type enzyme
Y281A/R282A/S283A
-
site-directed mutagenesis, highly reduced activity with pyruvate compared to the wild-type enzyme
Y281S/R282S
-
site-directed mutagenesis, highly reduced activity with pyruvate compared to the wild-type enzyme
D289A
-
the beta subunit mutant does not have any detectable activity in assays with NAD+ and shows no change in activity in 2,6-dichlorophenolindophenol assays
D289N
-
the beta subunit mutant shows by 36% reduced activity in assays with NAD+
E229A
-
the beta subunit mutant does not show drastic changes compared to the wild type E1 activities
E229Q
-
the beta subunit mutant does not show drastic changes compared to the wild type E1 activities
E232A
-
the beta subunit mutant does not show drastic changes compared to the wild type E1 activities
E232Q
-
the beta subunit mutant does not show drastic changes compared to the wild type E1 activities
E234A
-
the beta subunit mutant does not show drastic changes compared to the wild type E1 activities
E234Q
-
the beta subunit mutant does not show drastic changes compared to the wild type E1 activities
I329A
-
shows 37-43% reduction in activity compared to the wild type enzyme
R253G
-
the mutation is associated with low PDHc activity and absence of subunit alpha of pyruvate dehydrogenase E1
S264E
pseudophosphorylation mutant, the preceding binding of substrate to the enzyme's active site via the substrate channel and the subsequent reductive acetylation of the E2 component are severely slowed in the mutant enzyme
S264Q
selectively deficient in pyruvate binding and reductive acetylation of component E2
E401K
1.04% of overall wild type activity and 4.63% of wild type activity with 2,6-dichloroindolphenol
E401K
-
in the mutant, binding and reductive acetylation of E2p lipoyl domains are highly impaired
H407A
crystallization data. Interaction between H407 and phosphonolactylthiamine diphosphate is essential for stabilization of two loop regions in the active site
H407A
0.15% of overall wild type activity and 12.0% of wild type activity with 2,6-dichloroindolphenol
H407A
-
in the mutant, binding and reductive acetylation of E2p lipoyl domains are highly impaired
Y177A
-
11% of wild-type activity in enzyme complex
Y177A
-
in the mutant, binding and reductive acetylation of E2p lipoyl domains are highly impaired
additional information
-
construction of the iar4-1 mutant, defective in gene iar4 encoding the enzyme E1, by ethylmethane sulfonate, the mutant is less sensitive to a synthetic auxin and low concentrations of an ethylene precursor, but responds to free indole-3-acetic acid and other hormones in a way similar to the wild-type, the Krebs cycle and glycolysis are unaffected
additional information
-
genes bvPDH_E1alpha-2 and bvPDH_E1alpha-1 encode the type 2 and type 1 variants of the E1alpha subunit of pyruvate dehydrogenase, expression as GFP-fusion protein, antisense expression, using a tapetum-specific TA29 promotor in antisense orientation, of gene type 1 variant of the E1alpha subunit via infection with Agrobacterium tumefaciens to form transgenic tobacco plants, cv. SR-1, leads to decreased transcript and male sterility, abnormal anther phenotype, poorly formed microspores, overview
additional information
enzyme-deficient mutant. Inactivation of enzyme gene leads to the inability to grow on glucose and the absence of enzymic and enzyme complex activities
additional information
-
construction of several N-terminal E1 deletion mutants by tryptic or chymotryptic digest all showing reduced enzyme activity
additional information
-
mutant I329DELTA (deletion at the C-terminal of E1) shows 62% reduction in activity compared to the wild type enzyme
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Active-site changes in the pyruvate dehydrogenase multienzyme complex E1 apoenzyme component from Escherichia coli observed at 2.32 A resolution
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Homo sapiens
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Escherichia coli (P0AFG8), Escherichia coli
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Geobacillus stearothermophilus
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Escherichia coli
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Balakrishnan, A.; Nemeria, N.S.; Chakraborty, S.; Kakalis, L.; Jordan, F.
Determination of pre-steady-state rate constants on the Escherichia coli pyruvate dehydrogenase complex reveals that loop movement controls the rate-limiting step
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2012
Escherichia coli
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Chandrasekhar, K.; Wang, J.; Arjunan, P.; Sax, M.; Park, Y.H.; Nemeria, N.S.; Kumaran, S.; Song, J.; Jordan, F.; Furey, W.
Insight to the interaction of the dihydrolipoamide acetyltransferase (E2) core with the peripheral components in the Escherichia coli pyruvate dehydrogenase complex via multifaceted structural approaches
J. Biol. Chem.
288
15402-15417
2013
Escherichia coli
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