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2-oxobutanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
-
-
-
?
2-oxobutyrate + CoA + NAD+
propanoyl-CoA + CO2 + NADH + H+
-
-
-
-
r
2-oxoisovalerate + CoA + NAD+
isobutanoyl-CoA + CO2 + NADH
-
-
-
-
?
acetaldehyde + benzaldehyde
(R)-phenylacetylcarbinol
hydroxyethyl thiamine diphosphate + CoA + NAD+
? + NADH
-
-
-
-
?
pyruvate + acetylphosphinate + NAD+
(R)-acetoin + ? + NADH
-
-
-
-
?
pyruvate + acetylphosphinate + NAD+
(S)-acetoin + ? + NADH
-
-
-
-
?
pyruvate + CoA + dichlorophenol indophenol
acetyl-CoA + CO2 + ?
-
-
-
?
pyruvate + CoA + ferricyanide
acetyl-CoA + CO2 + ferrocyanide
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH + H+
pyruvate + CoA + oxidized 2,6-dichlorophenolindophenol
acetyl-CoA + CO2 + reduced 2,6-dichlorophenolindophenol
pyruvate + CoA + thiamine diphosphate
acetyl-CoA + CO2 + ?
-
-
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
pyruvate + lipoyl domain
acetylated lipoyl domain + CO2
-
-
-
-
r
pyruvate + N-acetyl-GDLLAEIETDK(lipoyl)-ATIG-amide
?
-
-
-
-
r
pyruvate + N-terminal lipoyl domain
?
-
-
-
-
r
pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine
[dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2
-
-
-
?
additional information
?
-
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
-
-
-
-
ir
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
-
ir
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
-
-
-
-
ir
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
ir
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 + H+
-
-
-
-
r
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH + H+
Pigeon
-
-
-
-
r
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH + H+
-
-
-
-
r
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH + H+
-
-
-
-
r
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
-
in overall reaction of pyruvate dehydrogenase complex, pyruvate can be replaced by 2-ketobutyrate
-
?
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 miso
-
in overall reaction of pyruvate dehydrogenase complex, pyruvate can be replaced by 2-ketobutyrate
-
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
Hansenula miso
-
low reactivity with 2-ketovalerate
-
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
Hansenula miso
-
additional reactions of complex, e. g. reduction of K3Fe(CN)6
-
-
?
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
-
in overall reaction of pyruvate dehydrogenase complex, pyruvate can be replaced by hydroxypyruvate
-
?
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 hydroxypyruvate
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
-
-
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
-
in overall reaction of pyruvate dehydrogenase complex, pyruvate can be replaced by hydroxypyruvate
-
?
additional information
?
-
non-complex-bound E1p shows the same cooperativity as found for complex-bound E1p. A Hill coefficient of 1.2-1.6 is calculated for non-complex bound E1p
-
-
-
additional information
?
-
-
E1 is bound to E2, both components of the pyruvate dehydrogenase multienzyme complex PDC, via the E1-binding B domain of E2, enzyme component organization in the pyruvate dehydrogenase multienzyme complex, regulatory role, overview
-
-
?
additional information
?
-
-
the PDH complex irreversibly decarboxylates pyruvate to acetylCoA (PDH activity) in a reaction that involves the participation of the three enzymes forming the PDH complex: AceE (pyruvate decarboxylase), AceF (dihydrolipoil acetyltransferase) and Lpd (dihydrolipoil dehydrogenase)
-
-
?
additional information
?
-
-
the PDH complex irreversibly decarboxylates pyruvate to acetylCoA (PDH activity) in a reaction that involves the participation of the three enzymes forming the PDH complex: AceE (pyruvate decarboxylase), AceF (dihydrolipoil acetyltransferase) and Lpd (dihydrolipoil dehydrogenase)
-
-
?
additional information
?
-
-
in vivo there are 20-30 E1 molecules bound to each core of the mammalian PDC, the small binding domain of E2 in humans binds only to E1
-
-
?
additional information
?
-
-
the pyruvate dehydrogenase complex consists of multiple copies of several components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2), dihydrolipoamide dehydrogenase (E3), E3-binding protein (BP), and specific kinases and phosphatases
-
-
?
additional information
?
-
pyruvate is a better substrate than 2-oxobutanoate, other 2-oxo-acids are not substrates
-
-
-
additional information
?
-
-
substrate interaction kinetics for all substrates are consistent with a multisite ping-pong mechanism
-
-
-
additional information
?
-
-
pyruvate-supported mitochondrial respiration state 3
-
-
?
additional information
?
-
-
substrate interaction kinetics for all substrates are consistent with a multisite ping-pong mechanism
-
-
-
additional information
?
-
-
regulation of pyruvate dehydrogenase complex activity and citric acid cycle intermediates during high cardiac power generation, inhibition of fatty acid oxidation has a regulatory function, overview
-
-
?
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pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
additional information
?
-
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
-
-
-
-
ir
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
-
-
-
-
ir
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
-
additional reactions of complex, e. g. reduction of K3Fe(CN)6
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
-
in overall reaction of pyruvate dehydrogenase complex, pyruvate can be replaced by 2-ketobutyrate
-
?
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 miso
-
in overall reaction of pyruvate dehydrogenase complex, pyruvate can be replaced by 2-ketobutyrate
-
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
Hansenula miso
-
low reactivity with 2-ketovalerate
-
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
Hansenula miso
-
additional reactions of complex, e. g. reduction of K3Fe(CN)6
-
-
?
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
-
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 hydroxypyruvate
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
-
-
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
-
in overall reaction of pyruvate dehydrogenase complex, pyruvate can be replaced by hydroxypyruvate
-
?
additional information
?
-
-
E1 is bound to E2, both components of the pyruvate dehydrogenase multienzyme complex PDC, via the E1-binding B domain of E2, enzyme component organization in the pyruvate dehydrogenase multienzyme complex, regulatory role, overview
-
-
?
additional information
?
-
-
the PDH complex irreversibly decarboxylates pyruvate to acetylCoA (PDH activity) in a reaction that involves the participation of the three enzymes forming the PDH complex: AceE (pyruvate decarboxylase), AceF (dihydrolipoil acetyltransferase) and Lpd (dihydrolipoil dehydrogenase)
-
-
?
additional information
?
-
-
the PDH complex irreversibly decarboxylates pyruvate to acetylCoA (PDH activity) in a reaction that involves the participation of the three enzymes forming the PDH complex: AceE (pyruvate decarboxylase), AceF (dihydrolipoil acetyltransferase) and Lpd (dihydrolipoil dehydrogenase)
-
-
?
additional information
?
-
-
the pyruvate dehydrogenase complex consists of multiple copies of several components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2), dihydrolipoamide dehydrogenase (E3), E3-binding protein (BP), and specific kinases and phosphatases
-
-
?
additional information
?
-
-
pyruvate-supported mitochondrial respiration state 3
-
-
?
additional information
?
-
-
regulation of pyruvate dehydrogenase complex activity and citric acid cycle intermediates during high cardiac power generation, inhibition of fatty acid oxidation has a regulatory function, overview
-
-
?
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1-(4-bromophenyl)ethanone O-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-1H-1,2,3-triazol-4-yl)methyl)oxime
thiamine diphosphate analog, at 0.1 mM 33% inhibition against Gibberlla zeae
1-(4-chlorophenyl)ethanone O-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-1H-1,2,3-triazol-4-yl)methyl)oxime
thiamine diphosphate analog, at 0.1 mM 35% inhibition against Gibberlla zeae
1-(4-nitrophenyl)ethanone O-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-1H-1,2,3-triazol-4-yl)methyl)oxime
thiamine diphosphate analog, at 0.1 mM 50% inhibition against Gibberlla zeae
1-[3-[4-(1,3,2-dithiarsinan-2-yl)anilino]-3-oxopropyl]-4-[(E)-2-(1H-indol-3-yl)ethenyl]pyridin-1-ium
i.e. PDT-PAO-16, organic arsenal inhibitor, mainly accumulates in mitochondria within hours and suppresses the activity of the pyruvate dehydrogenase complex resulting in the inhibition of ATP synthesis and thermogenesis disorder. The suppression of respiratory chain complex I and IV accelerates the mitochondrial dysfunction leading to caspase family-dependent apoptosis. In vivo, the acute promyelocytic leukemia is greatly alleviated in the PDT-PAO-F16 treated group in an acute promyelocytic leukemia mice model
2,3-Butanedione
Pigeon
-
10 mM, biphasic kinetic, complete inactivation after 20 min
2-([1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-iodo-4,5-dihydro-1H-1,2,3-triazol-4-yl]methyl)-1H-isoindole-1,3(2H)-dione
potent algaecidal activity against Synechocystis sp. PCC 6803
2-p-Toluidinonaphthalene-6-sulfonate
-
-
3-([1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4,5-dihydro-1H-1,2,3-triazol-4-yl]methyl)-5-chloroquinazolin-4(3H)-one
-
3-([1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4,5-dihydro-1H-1,2,3-triazol-4-yl]methyl)-6-bromoquinazolin-4(3H)-one
-
3-([1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-iodo-4,5-dihydro-1H-1,2,3-triazol-4-yl]methyl)-6-bromoquinazolin-4(3H)-one
potent algaecidal activity against Synechocystis sp. PCC 6803
3-([1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-iodo-4,5-dihydro-1H-1,2,3-triazol-4-yl]methyl)-6-chloro-1,2,3-benzotriazin-4(3H)-one
-
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
4-aminophenyl arsenoxide
0.1 mM, 92% loss of activity in presence of pyruvate and CoA. Controls lacking pyruvate and/or coenzyme A, but containing H2NPhAsO, retain nearly all their pyruvate dehydrogenase complex activity. The arsenoxide forms a stable cyclic dithiolarsinite with reduced lipoic acid on E2 which is generated by pyruvate and coenzyme A according. Pyruvate dehydrogenase complex activity can be recovered to 78% within 2 min following the addition of 2,3-dithiopropanol
5,5'-dithiobis(2-nitrobenzoate)
Pigeon
-
-
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
-
exhibits activity against Rhizoctonia solani even at 12.5 lg/ml and almost 5.5 times more inhibitory potency against Botryttis cinerea than pyrimethanil
alpha-Ketobutyric acid
-
-
alpha-ketooctanoic acid
-
-
bromoacetylaniline arsenoxide
BrCH2CONHPhAsO, 0.1 mM, 100% loss of activity in presence of pyruvate and CoA. The initial reaction of the bifunctional reagent occurs on E2 via the R-AsO moiety and results in the rapid loss in pyruvate dehydrogenase complex activity. Addition of 2,3-dithiopropanol fails to regenerate the complex activity and E3 activity
citrate
-
0.25 mM, 29% inhibition, 50.0 mM, 87% inhibition
CoA
allosteric inhibition
CuSO4
EC50 value against Synechocystis sp. PCC 6803 is 0.002 mM
diethyldicarbonate
Pigeon
-
-
gibberellin
-
modulates the activity of enzyme by regulating the expression of pyruvate dehydrogenase kinase1 and subsequently controlling plant growth and development
GTP
-
5 mM, about 50% inhibition after 3 h
Guanidinium chloride
-
treatment of the E2-X subcomplex with 4 M guanidinium chloride causes a complete loss of enzymatic activity and the dissociation of the subcomplex into monomeric 1.5-3 S species. Removal of the chaotrope by dialysis for 18 h results in complete restoration of E2 enzymatic activity and reassembly of a 32 S subcomplex. The reassembled E2-X subcomplex demonstrates the presence of an 8 S assembly intermediate. The 8 S species associates non-cooperatively to yield additional assembly intermediates exhibiting sedimentation coefficients of 10-32 S
illumination
-
mitochondrial pyruvate dehydrogenase complex
-
Moniliformin
-
0.3 mM, 82% inhibition
N-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-1H-1,2,3-triazol-4-yl) methyl)-2,4,6-trimethylbenzenesulfonamide
thiamin 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
thiamin 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
thiamin 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
thiamin 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
thiamin 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
thiamin 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
thiamin 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
thiamin 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
thiamin diphosphate analogue, EC50 value against Synechocystis sp. PCC 6803 is 0.0016 mM, EC50 value against Microcystis aeruginosa FACHB905 is 0.0001 mM
-
N-(3-[(2E)-2-[(4-amino-2-methylpyrimidin-5-yl)methylidene]hydrazinecarbonyl]phenyl)-2-fluorobenzamide
72-92% inhibition against Xanthomonas oryzae pv. Oryzae and Ralstonia solanacearum at 100 microg/ml
N-(3-[(2E)-2-[(4-amino-2-methylpyrimidin-5-yl)methylidene]hydrazinecarbonyl]phenyl)-4-bromobenzamide
negligible inhibition against porcine pyruzvate dehydrogenase complex, 72-92% inhibition against Xanthomonas oryzae pv. Oryzae and Ralstonia solanacearum at 100 microg/ml
N-(3-[(2E)-2-[(4-amino-2-methylpyrimidin-5-yl)methylidene]hydrazinecarbonyl]phenyl)-4-fluorobenzamide
72-92% inhibition against Xanthomonas oryzae pv. Oryzae and Ralstonia solanacearum at 100 microg/ml
N-(3-[(2E)-2-[(4-amino-2-methylpyrimidin-5-yl)methylidene]hydrazinecarbonyl]phenyl)-4-methylbenzamide
negligible inhibition against porcine pyruzvate dehydrogenase complex
N-(3-[(2E)-2-[(4-amino-2-methylpyrimidin-5-yl)methylidene]hydrazinecarbonyl]phenyl)butanamide
72-92% inhibition against Xanthomonas oryzae pv. Oryzae and Ralstonia solanacearum at 100 microg/ml
N-(4-[(2E)-2-[(4-amino-2-methylpyrimidin-5-yl)methylidene]hydrazinecarbonyl]phenyl)-4-bromobenzamide
negligible inhibition against porcine pyruzvate dehydrogenase complex
N-(4-[(2E)-2-[(4-amino-2-methylpyrimidin-5-yl)methylidene]hydrazinecarbonyl]phenyl)-N'-phenylurea
negligible inhibition against porcine pyruzvate dehydrogenase complex, 72-92% inhibition against Xanthomonas oryzae pv. Oryzae and Ralstonia solanacearum at 100 microg/ml
p-chloromercuribenzoate
Pigeon
-
0.026 mM, complete inactivation after 80 s
PDC kinase II
-
phosphorylates and inactivates Pda1p
-
Phenylglyoxal
Pigeon
-
10 mM, biphasic kinetic, complete inactivation after 30 min
protein Pkp1p
-
phosphorylates and inactivates Pda1p
-
Pyruvamide
-
acts as substrate analogue, competitive
pyruvate dehydrogenase kinase
-
deactivates PDH by phosphorylation
-
Sodium diphosphate
-
competitive vs. thiamine diphosphate
tellurite
-
pyruvate dehydrogenase activity decreases by 81% after tellurite treatment (0.0005 mg/ml for 30 min)
thiamin 2-thiazolone diphosphate
tight-binding inhibitor, binds via a two-step mechanism,
thiamin 2-thiothiazolone diphosphate
tight-binding inhibitor, binds via a two-step mechanism to wild-type, but to mutant Y177A via a one-step mechanism
thiamine 2-thiothiazolone diphosphate
-
-
tryptamine-4,5-dione
-
inhibition is blocked by reduced glutathione or cysteine at large molar excess, ascorbate protects partially
[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-iodo-4,5-dihydro-1H-1,2,3-triazol-4-yl]methyl 3-chlorobenzoate
-
[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-iodo-4,5-dihydro-1H-1,2,3-triazol-4-yl]methyl 4-chlorobenzoate
compound shows inhibitory selectivity between Synechocystis sp. pyruvate dehydrogenase complex E1 (inhibitory rate 98.90%) and porcine pyruvate dehydrogenase complex E1 (inhibitory rate 9.54%)
[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-iodo-4,5-dihydro-1H-1,2,3-triazol-4-yl]methyl 4-fluorobenzoate
-
[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-iodo-4,5-dihydro-1H-1,2,3-triazol-4-yl]methyl 4-nitrobenzoate
-
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
acetyl-CoA
product inhibition, apart from interaction with the active site on subunit E2p, acetyl CoA interacts directly with the E1p component
acetyl-CoA
-
reversed by CoA
acetyl-CoA
-
uncompetitive with respect to pyruvate, noncompetitive with respect to CoA and NAD+
acetyl-CoA
-
uncompetitive with respect to pyruvate, noncompetitive with respect to CoA and NAD+
acetylmethylphosphinate
-
partially reversible tight-binding inhibitor, formation of a C2alpha-phosphinolactylthiamine diphosphate derivative involving H63 residue of enzyme
acetylmethylphosphinate
-
partially reversible tight-binding inhibitor, formation of a C2alpha-phosphinolactylthiamine diphosphate derivative involving H63 residue of enzyme
Acetylphosphinate
-
partially reversible tight-binding inhibitor, formation of a C2alpha-phosphinolactylthiamine diphosphate derivative involving H63 residue of enzyme
Acetylphosphinate
-
partially reversible tight-binding inhibitor, formation of a C2alpha-phosphinolactylthiamine diphosphate derivative involving H63 residue of enzyme
beta-Hydroxypyruvate
-
competitive vs. pyruvate
beta-Hydroxypyruvate
-
noncompetitive vs. pyruvate
Fluoropyruvate
-
acts as substrate analogue, competitive
Fluoropyruvate
-
irreversible, protection by dihydrolipoamide
glyoxylate
-
noncompetitive vs. pyruvate
glyoxylate
-
competitive vs. pyruvate
glyoxylate
inhibitory only in the absence of thiol reagents, competitive with respect to pyruvate
MgATP2-
-
5 mM, about 70% inhibition after 3 h
MgATP2-
-
5 mM, 93% inhibition due to phosphorylation
NADH
-
-
NADH
-
competitive with respect to NAD+, noncompetitive with respect to CoA and pyruvate
NADH
-
mixed type inhibition
NADH
-
competitive with respect to NAD+, noncompetitive with respect to CoA and pyruvate
Oxythiamine diphosphate
-
competitive inhibitor, shows a significant cytostatic effect on HeLa cell culture
Oxythiamine diphosphate
-
competitive inhibitor
phosphorylation
-
-
-
additional information
-
not inhibited by ATP
-
additional information
-
not inhibited by ATP
-
additional information
-
PDH activity can be downregulated by an increase in dietary fat, attenuated PHD contributes to the preferential oxidation of n-6 poly unsaturated fatty acids during moderate-intensity exercis
-
additional information
-
pyruvate dehydrogenase complex inhibition occurs via enhanced expression of pyruvate dehydrogenase kinase-1, which results in inhibitory phosphorylation of the pyruvate dehydrogenase alpha subunit, knockdown of pyruvate dehydrogenase kinase-1 via short hairpin RNA lowers inhibitory PDHalpha phosphorylation
-
additional information
-
not inhibited by ATP
-
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Abscess
Regulation of glucose metabolism by altered pyruvate dehydrogenase activity. I. Potential site of insulin resistance in sepsis.
Acidosis, Lactic
Absence of pyruvate decarboxylase activity in man: a cause of congenital lactic acidosis.
Acidosis, Lactic
Characterization of two cDNA clones for pyruvate dehydrogenase E1 beta subunit and its regulation in tricarboxylic acid cycle-deficient fibroblast.
Acidosis, Lactic
Immunochemical analysis of normal and mutant forms of human pyruvate dehydrogenase.
Acidosis, Lactic
Pyruvate dehydrogenase (PDH) deficiency caused by a 21-base pair insertion mutation in the E1 alpha subunit.
Acidosis, Lactic
Unilateral periventricular leukomalacia in association with pyruvate dehydrogenase deficiency.
Acidosis, Lactic
[Pyruvate dehydrogenase deficiency and cerebral malformations]
Ataxia
Familial intermittent ataxia due to a defect of the E1 component of pyruvate dehydrogenase complex.
Ataxia
Immunochemical analysis of pyruvate dehydrogenase complex in 2 boys with primary lactic acidemia.
Ataxia
Pyruvate dehydrogenase deficiency in spinocerebellar degenerations.
Brain Diseases
Cerebral palsy and pyruvate dehydrogenase deficiency: identification of two new mutations in the E1alpha gene.
Breast Neoplasms
The Effects of Thiamine on Breast Cancer Cells.
Cytochrome-c Oxidase Deficiency
Nonviability of cells with oxidative defects in galactose medium: a screening test for affected patient fibroblasts.
dihydrolipoyl dehydrogenase deficiency
Novel mutations in dihydrolipoamide dehydrogenase deficiency in two cousins with borderline-normal PDH complex activity.
Friedreich Ataxia
Friedreich's ataxia II. Biochemical studies in cultured cells.
Friedreich Ataxia
Friedreich's ataxia in northern Italy. II. Biochemical studies in cultured cells.
Glucose Intolerance
"In vitro" effects of insulin on the PDH complex of the isolated perfused heart of rats fed a sucrose-rich diet.
Heart Failure
Adaptations in Protein Expression and Regulated Activity of Pyruvate Dehydrogenase Multienzyme Complex in Human Systolic Heart Failure.
Heart Failure, Systolic
Adaptations in Protein Expression and Regulated Activity of Pyruvate Dehydrogenase Multienzyme Complex in Human Systolic Heart Failure.
Hepatitis
Autoreactive liver-infiltrating T cells in primary biliary cirrhosis recognize inner mitochondrial epitopes and the pyruvate dehydrogenase complex.
Hepatitis, Autoimmune
Autoreactive liver-infiltrating T cells in primary biliary cirrhosis recognize inner mitochondrial epitopes and the pyruvate dehydrogenase complex.
Hyperlactatemia
Potentiation of decreased pyruvate dehydrogenase activity by inflammatory stimuli in sepsis.
Hyperlactatemia
TNF binding protein prevents hyperlactatemia and inactivation of PDH complex in skeletal muscle during sepsis.
Infections
Potentiation of decreased pyruvate dehydrogenase activity by inflammatory stimuli in sepsis.
Insulin Resistance
Effect of starvation and insulin in vivo on the activity of the pyruvate dehydrogenase complex in rat skeletal muscles.
Insulin Resistance
Pyruvate dehydrogenase-complex activity in brown adipose tissue of gold thioglucose-obese mice.
Intellectual Disability
Immunochemical analysis of pyruvate dehydrogenase complex in 2 boys with primary lactic acidemia.
Kearns-Sayre Syndrome
Nonviability of cells with oxidative defects in galactose medium: a screening test for affected patient fibroblasts.
Lewy Body Disease
Alteration of mitochondrial protein PDHA1 in Lewy body disease and PARK14.
Metabolism, Inborn Errors
Pyruvate dehydrogenase complex deficiency caused by ubiquitination and proteasome-mediated degradation of the E1 subunit.
Microcephaly
Cerebral palsy and pyruvate dehydrogenase deficiency: identification of two new mutations in the E1alpha gene.
nadh:ubiquinone reductase (h+-translocating) deficiency
Neonatal onset of mitochondrial disorders in 129 patients: clinical and laboratory characteristics and a new approach to diagnosis.
Neoplasms
Pyruvate dehydrogenase complex activity controls metabolic and malignant phenotype in cancer cells.
Nervous System Diseases
Alteration of mitochondrial protein PDHA1 in Lewy body disease and PARK14.
Obesity
Inactivation of pyruvate dehydrogenase complex in heart muscle mitochondria of gold-thioglucose-induced obese mice is not due to a stable increase in activity of pyruvate dehydrogenase kinase.
Optic Nerve Diseases
Nonviability of cells with oxidative defects in galactose medium: a screening test for affected patient fibroblasts.
Pituitary Neoplasms
Differential effects of metformin on reductive activity and energy production in pituitary tumor cells compared to myogenic precursors.
pyruvate dehydrogenase (acetyl-transferring) deficiency
Cerebral palsy and pyruvate dehydrogenase deficiency: identification of two new mutations in the E1alpha gene.
Pyruvate Dehydrogenase Complex Deficiency Disease
Cerebral palsy and pyruvate dehydrogenase deficiency: identification of two new mutations in the E1alpha gene.
pyruvate dehydrogenase system deficiency
Analysis of exonic mutations leading to exon skipping in patients with pyruvate dehydrogenase E1 alpha deficiency.
pyruvate dehydrogenase system deficiency
Cerebral palsy and pyruvate dehydrogenase deficiency: identification of two new mutations in the E1alpha gene.
pyruvate dehydrogenase system deficiency
Deficiency of pyruvate dehydrogenase caused by novel and known mutations in the E1alpha subunit.
pyruvate dehydrogenase system deficiency
Diagnosis of partial deficiency of the pyruvate dehydrogenase complex in biopsied muscle.
pyruvate dehydrogenase system deficiency
Mutation analysis of the pyruvate dehydrogenase E1 alpha gene in eight patients with a pyruvate dehydrogenase complex deficiency.
pyruvate dehydrogenase system deficiency
Mutations in the X-linked E1 alpha subunit of pyruvate dehydrogenase leading to deficiency of the pyruvate dehydrogenase complex.
pyruvate dehydrogenase system deficiency
Mutations in the X-linked pyruvate dehydrogenase (E1) alpha subunit gene (PDHA1) in patients with a pyruvate dehydrogenase complex deficiency.
pyruvate dehydrogenase system deficiency
Neonatal onset of mitochondrial disorders in 129 patients: clinical and laboratory characteristics and a new approach to diagnosis.
pyruvate dehydrogenase system deficiency
Nonviability of cells with oxidative defects in galactose medium: a screening test for affected patient fibroblasts.
pyruvate dehydrogenase system deficiency
Phenotypic and Neuropathological Characterization of Fetal Pyruvate Dehydrogenase Deficiency.
pyruvate dehydrogenase system deficiency
Sequential deletion of C-terminal amino acids of the E(1)alpha component of the pyruvate dehydrogenase (PDH) complex leads to reduced steady-state levels of functional E(1)alpha(2)beta(2) tetramers: implications for patients with PDH deficiency.
Quadriplegia
Cerebral palsy and pyruvate dehydrogenase deficiency: identification of two new mutations in the E1alpha gene.
Sarcopenia
Abnormalities of mitochondrial functioning can partly explain the metabolic disorders encountered in sarcopenic gastrocnemius.
Seizures
Cerebral palsy and pyruvate dehydrogenase deficiency: identification of two new mutations in the E1alpha gene.
Sepsis
Potentiation of decreased pyruvate dehydrogenase activity by inflammatory stimuli in sepsis.
Sepsis
Regulation of glucose metabolism by altered pyruvate dehydrogenase activity. I. Potential site of insulin resistance in sepsis.
Sepsis
Sepsis alters pyruvate dehydrogenase kinase activity in skeletal muscle.
Sepsis
Sepsis-induced alterations in pyruvate dehydrogenase complex activity in rat skeletal muscle: effects on plasma lactate.
Sepsis
TNF binding protein prevents hyperlactatemia and inactivation of PDH complex in skeletal muscle during sepsis.
Spinocerebellar Degenerations
Pyruvate dehydrogenase deficiency in spinocerebellar degenerations.
Starvation
Effect of starvation and insulin in vivo on the activity of the pyruvate dehydrogenase complex in rat skeletal muscles.
Starvation
Glucose fatty acid interactions and the regulation of glucose disposal.
Starvation
Inactivation of pyruvate dehydrogenase complex in heart muscle mitochondria of gold-thioglucose-induced obese mice is not due to a stable increase in activity of pyruvate dehydrogenase kinase.
Starvation
Insulin activation of pyruvate dehydrogenase complex is enhanced by exercise training.
Starvation
Kinase activator protein mediates longer-term effects of starvation on activity of pyruvate dehydrogenase kinase in rat liver mitochondria.
Starvation
Nutritional regulation of the protein kinases responsible for the phosphorylation of the alpha-ketoacid dehydrogenase complexes.
Starvation
Pyruvate dehydrogenase-complex activity in brown adipose tissue of gold thioglucose-obese mice.
Starvation
Reversible phosphorylation of pyruvate dehydrogenase in rat skeletal-muscle mitochondria. Effects of starvation and diabetes.
Starvation
Studies on the interactions of Ca2+ and pyruvate in the regulation of rat heart pyruvate dehydrogenase activity. Effects of starvation and diabetes.
Usher Syndromes
Cannabinoid Receptor 1 associates to different molecular complexes during GABAergic neuron maturation.
[pyruvate dehydrogenase (acetyl-transferring)] kinase deficiency
Fasting induces ketoacidosis and hypothermia in PDHK2/PDHK4 double knockout mice.
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1.35
2-oxobutanoate
pH 7.6, 22°C
1.27
2-oxoisovalerate
-
pH 7.0, 30°C
0.003
coenzyme A
-
assay with whole enzyme complex
0.0082
hydroxyethyl thiamine diphosphate
-
pH not specified in the publication, temperature not specified in the publication
0.36
Mg2+
-
whole enzyme complex
15
N-acetyl-GDLLAEIETDK(lipoyl)-ATIG-amide
-
-
0.052
N-terminal lipoyl domain
-
-
-
0.00008 - 0.05
thiamine diphosphate
additional information
additional information
-
0.0005
CoA
-
pH 7.4, 30°C
0.004
CoA
-
2-oxoglutarate dehydrogenase complex, pH 7.6, 30°C, in presence of thiamine diphosphate
0.004
CoA
-
pH not specified in the publication, temperature not specified in the publication
0.0046
CoA
-
pH not specified in the publication, temperature not specified in the publication
0.012
CoA
-
2-oxoglutarate dehydrogenase complex, pH 7.6, 30°C, in absence of thiamine diphosphate
0.0132
CoA
-
absence of malate, pH 7.6, temperature not specified in the publication
0.017
CoA
-
S0.5 value, pH 7.0, 25°C
0.019
CoA
-
domestic pig, pH 7.5, temperature not specified in the publication
0.0761
CoA
-
wild boar, pH 7.5, temperature not specified in the publication
0.61
CoA
-
presence of 1 mM malate, pH 7.6, temperature not specified in the publication
0.01
NAD+
-
pH 7.4, 30°C
0.022
NAD+
-
wild boar, pH 7.5, temperature not specified in the publication
0.033
NAD+
-
2-oxoglutarate dehydrogenase complex, pH 7.6, 30°C, in presence of thiamine diphosphate
0.0336
NAD+
-
domestic pig, pH 7.5, temperature not specified in the publication
0.051
NAD+
-
assay with whole enzyme complex
0.07
NAD+
-
2-oxoglutarate dehydrogenase complex, pH 7.6, 30°C, in absence of thiamine diphosphate
0.076
NAD+
-
absence of malate, pH 7.6, temperature not specified in the publication
0.1
NAD+
-
pH not specified in the publication, temperature not specified in the publication
0.136
NAD+
-
presence of 1 mM malate, pH 7.6, temperature not specified in the publication
0.238
NAD+
-
pH not specified in the publication, temperature not specified in the publication
0.0002
pyruvate
-
2-oxoglutarate dehydrogenase complex, pH 7.6, 30°C, in presence of thiamine diphosphate, in presence of 2 mM Mn2+
0.0006
pyruvate
-
2-oxoglutarate dehydrogenase complex, pH 7.6, 30°C, in presence of thiamine diphosphate, in presence of 2 mM Ca2+
0.0006
pyruvate
-
cooperativity is observed, Hill coefficient is 1.6, pH 7.6, 37°C
0.0007
pyruvate
-
2-oxoglutarate dehydrogenase complex, pH 7.6, 30°C, in absence of thiamine diphosphate, in presence of 2 mM Mn2+
0.0016
pyruvate
-
2-oxoglutarate dehydrogenase complex, pH 7.6, 30°C, in absence of thiamine diphosphate, in presence of 2 mM Ca2+
0.002
pyruvate
-
value is 0.002 to 0.004, pH 7.4, 30°C
0.0043
pyruvate
-
domestic pig, pH 7.5, temperature not specified in the publication
0.01
pyruvate
E1 component, pH 7.6, 30°C
0.0124
pyruvate
pH 7.2, 37°C
0.0153
pyruvate
-
wild boar, pH 7.5, temperature not specified in the publication
0.017
pyruvate
Pigeon
-
-
0.017
pyruvate
-
similar values
0.02
pyruvate
patient with primary lactic acidaemia, pH 8.0, temperature not specified in the publication
0.0226
pyruvate
-
pH 7.0, 37°C, mutant S271A of isoform PDH2
0.023
pyruvate
-
2-oxoglutarate dehydrogenase complex, pH 7.6, 30°C, in presence of thiamine diphosphate, without divalent cations
0.0258
pyruvate
-
pH 7.0, 37°C, mutant S271E of isoform PDH2
0.0263
pyruvate
-
pH 7.0, 37°C, mutant S203A of isoform PDH2
0.027
pyruvate
-
pH 7.6, 30°C, catalytic subunit E1
0.0359
pyruvate
-
pH 7.0, 37°C, isoform PDH2
0.053
pyruvate
-
pH not specified in the publication, temperature not specified in the publication
0.056
pyruvate
presence of 0.002 mM inhibitor N-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-5-iodo-1H-1,2,3-triazol-4-yl)methyl)-4-nitrobenzenesulfonamide, pH 7.2, 37°C
0.0565
pyruvate
-
pH 7.0, 37°C, mutant S203E of isoform PDH2
0.0567
pyruvate
pH 7.6, 22°C
0.058
pyruvate
healthy control, pH 8.0, temperature not specified in the publication
0.062
pyruvate
pH 7.5, 25°C
0.063
pyruvate
-
2-oxoglutarate dehydrogenase complex, pH 7.6, 30°C, in absence of thiamine diphosphate and divalent cations
0.0648
pyruvate
-
pH 7.0, 37°C, isoform PDH1
0.072
pyruvate
-
pH 7.6, 30°C, overall reaction of complex
0.072
pyruvate
-
pH not specified in the publication, temperature not specified in the publication
0.09
pyruvate
-
assay with whole enzyme complex
0.1
pyruvate
-
pH 7.5, 25°C
0.117
pyruvate
-
pH 7.0, 30°C
0.123
pyruvate
-
absence of malate, pH 7.6, temperature not specified in the publication
0.128
pyruvate
-
presence of 1 mM malate, pH 7.6, temperature not specified in the publication
0.14
pyruvate
-
assay with whole enzyme complex
0.2
pyruvate
-
pH 7.0, 25°C
0.28
pyruvate
mutant Y177A, pH 7.0, 30°C
0.32
pyruvate
-
pH 7.4, 30°C
0.515
pyruvate
wild-type, pH 7.0, 30°C
0.531
pyruvate
mutant Y177F, pH 7.0, 30°C
0.65
pyruvate
-
assay with whole enzyme complex
1
pyruvate
-
the complex displays cooperativity, Hill coefficient is 0.7, pH not specified in the publication, temperature not specified in the publication
0.00008
thiamine diphosphate
-
whole enzyme complex
0.00158
thiamine diphosphate
wild-type, Hill coefficient 1.38, pH 7.0, 30°C
0.00665
thiamine diphosphate
mutant Y177A, Hill coefficient 1.0, pH 7.0, 30°C
0.05
thiamine diphosphate
-
-
additional information
additional information
-
kinetic and thermodynamic analysis
-
additional information
additional information
-
kinetic study, reaction of pyruvate dehydrogenase complex
-
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0.0061 - 0.0069
1-(4-bromophenyl)ethanone O-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-1H-1,2,3-triazol-4-yl)methyl)oxime
0.0067
1-(4-nitrophenyl)ethanone O-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-1H-1,2,3-triazol-4-yl)methyl)oxime
Escherichia coli
pH 6.4, 37°C
0.0059
2-([1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-iodo-4,5-dihydro-1H-1,2,3-triazol-4-yl]methyl)-1H-isoindole-1,3(2H)-dione
Escherichia coli
pH 6.4, 37°C
0.00212
3-([1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4,5-dihydro-1H-1,2,3-triazol-4-yl]methyl)-5-chloroquinazolin-4(3H)-one
Escherichia coli
pH 6.4, 37°C
0.0043
3-([1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4,5-dihydro-1H-1,2,3-triazol-4-yl]methyl)-6-bromoquinazolin-4(3H)-one
Escherichia coli
pH 6.4, 37°C
8.21
3-([1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-iodo-4,5-dihydro-1H-1,2,3-triazol-4-yl]methyl)-6-bromoquinazolin-4(3H)-one
Escherichia coli
pH 6.4, 37°C
0.00362
3-([1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-iodo-4,5-dihydro-1H-1,2,3-triazol-4-yl]methyl)-6-chloro-1,2,3-benzotriazin-4(3H)-one
Escherichia coli
pH 6.4, 37°C
0.0000026
3-deazathiamine diphosphate
Sus scrofa
-
pH 7.8, temperature not specified in the publication
0.0101
4-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-5-iodo-1H-1,2,3-triazol-4-yl)methoxy)benzonitrile
Escherichia coli
-
isolated E1 component, pH 6.5, 37°C
0.0042
5-((4-((4-bromophenoxy)methyl)-5-iodo-1H-1,2,3-triazol-1-yl)methyl)-2-methylpyrimidin-4-amine
Escherichia coli
-
isolated E1 component, pH 6.5, 37°C
0.0051
5-((4-((4-chloro-3-methylphenoxy)methyl)-5-iodo-1H-1,2,3-triazol-1-yl)methyl)-2-methylpyrimidin-4-amine
Escherichia coli
-
isolated E1 component, pH 6.5, 37°C
0.0118
5-((4-((4-chlorophenoxy)methyl)-5-iodo-1H-1,2,3-triazol-1-yl)methyl)-2-methylpyrimidin-4-amine
Escherichia coli
-
isolated E1 component, pH 6.5, 37°C
0.0094
N-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-1H-1,2,3-triazol-4-yl) methyl)-2,4,6-trimethylbenzenesulfonamide
Synechocystis sp. PCC 6803
pH 7.2, 37°C
-
0.0046
N-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-1H-1,2,3-triazol-4-yl) methyl)-2-nitrobenzenesulfonamide
Synechocystis sp. PCC 6803
pH 7.2, 37°C
-
0.0088
N-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-1H-1,2,3-triazol-4-yl) methyl)-4-bromobenzenesulfonamide
Synechocystis sp. PCC 6803
pH 7.2, 37°C
-
0.0071
N-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-5-iodo-1H-1,2,3-triazol-4-yl) methyl)-4-chlorobenzenesulfonamide
Synechocystis sp. PCC 6803
pH 7.2, 37°C
-
0.0068
N-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-5-iodo-1H-1,2,3-triazol-4-yl)methyl)-2,4,6-trimethylbenzenesulfonamide
Synechocystis sp. PCC 6803
pH 7.2, 37°C
-
0.0078
N-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-5-iodo-1H-1,2,3-triazol-4-yl)methyl)-4-bromobenzenesulfonamide
Synechocystis sp. PCC 6803
pH 7.2, 37°C
-
0.0086
N-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-5-iodo-1H-1,2,3-triazol-4-yl)methyl)-4-fluorobenzenesulfonamide
Synechocystis sp. PCC 6803
pH 7.2, 37°C
-
0.0037
N-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-5-iodo-1H-1,2,3-triazol-4-yl)methyl)-4-methoxybenzenesulfonamide
Synechocystis sp. PCC 6803
pH 7.2, 37°C
-
0.0096
N-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-5-iodo-1H-1,2,3-triazol-4-yl)methyl)-4-methylbenzenesulfonamide
Synechocystis sp. PCC 6803
pH 7.2, 37°C
-
0.0035
N-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-5-iodo-1H-1,2,3-triazol-4-yl)methyl)-4-nitrobenzenesulfonamide
Synechocystis sp. PCC 6803
pH 7.2, 37°C
-
0.00237
N-(3-[(2E)-2-[(4-amino-2-methylpyrimidin-5-yl)methylidene]hydrazinecarbonyl]phenyl)-2-fluorobenzamide
Escherichia coli
pH 6.4, 37°C
0.00066
N-(3-[(2E)-2-[(4-amino-2-methylpyrimidin-5-yl)methylidene]hydrazinecarbonyl]phenyl)-4-bromobenzamide
Escherichia coli
pH 6.4, 37°C
0.00191
N-(3-[(2E)-2-[(4-amino-2-methylpyrimidin-5-yl)methylidene]hydrazinecarbonyl]phenyl)-4-fluorobenzamide
Escherichia coli
pH 6.4, 37°C
0.00285
N-(3-[(2E)-2-[(4-amino-2-methylpyrimidin-5-yl)methylidene]hydrazinecarbonyl]phenyl)-4-methylbenzamide
Escherichia coli
pH 6.4, 37°C
0.00469
N-(3-[(2E)-2-[(4-amino-2-methylpyrimidin-5-yl)methylidene]hydrazinecarbonyl]phenyl)butanamide
Escherichia coli
pH 6.4, 37°C
0.00062
N-(4-[(2E)-2-[(4-amino-2-methylpyrimidin-5-yl)methylidene]hydrazinecarbonyl]phenyl)-4-bromobenzamide
Escherichia coli
pH 6.4, 37°C
0.00054
N-(4-[(2E)-2-[(4-amino-2-methylpyrimidin-5-yl)methylidene]hydrazinecarbonyl]phenyl)-N'-phenylurea
Escherichia coli
pH 6.4, 37°C
0.000025
Oxythiamine diphosphate
Sus scrofa
-
pH 7.8, temperature not specified in the publication
0.00179
[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-iodo-4,5-dihydro-1H-1,2,3-triazol-4-yl]methyl 3-chlorobenzoate
Synechocystis sp. PCC 6803
isolated E1 component, pH 7.2, 37°C
0.00148
[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-iodo-4,5-dihydro-1H-1,2,3-triazol-4-yl]methyl 4-chlorobenzoate
Synechocystis sp. PCC 6803
isolated E1 component, pH 7.2, 37°C
0.00161
[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-iodo-4,5-dihydro-1H-1,2,3-triazol-4-yl]methyl 4-fluorobenzoate
Synechocystis sp. PCC 6803
isolated E1 component, pH 7.2, 37°C
0.00169
[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-iodo-4,5-dihydro-1H-1,2,3-triazol-4-yl]methyl 4-nitrobenzoate
Synechocystis sp. PCC 6803
isolated E1 component, pH 7.2, 37°C
0.0061
1-(4-bromophenyl)ethanone O-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-1H-1,2,3-triazol-4-yl)methyl)oxime
Escherichia coli
pH 6.4, 37°C
0.0069
1-(4-bromophenyl)ethanone O-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-1H-1,2,3-triazol-4-yl)methyl)oxime
Escherichia coli
pH 6.4, 37°C
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-
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brenda
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brenda
microsporidia, uncertain whether pyruvate dehydrogenase is used in acetyl-CoA synthesis and whether the entire pyruvate dehydrogenase complex is present in microsporidia
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
Q8NNF6 i.e. component E1, cf. EC 1.2.42, Q8NNJ2 i.e. component E2, cf. EC 2.3.1.61, Q8NTE1 i.e. component E3, cf. EC 1.8.1.4
UniProt
brenda
E1 component subunit alpha, cf. EC 1.2.4.1
UniProt
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
subspecies Fundulus heteroclitus heteroclitus
-
-
brenda
Hansenula miso
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
dihydrolipoyllysine-residue acetyltransferase component, cf. EC 2.3.1.12
UniProt
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
Pigeon
-
-
-
brenda
organism contains only one single enzyme complex
-
-
brenda
-
-
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brenda
-
-
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brenda
-
-
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brenda
-
-
-
brenda
-
-
-
brenda
spinach
-
-
brenda
Thermochaetoides thermophila
G0SHF3 i.e. E1 subunit alpha, G0RYE0 i.e. E1 subunit beta
UniProt
brenda
Thermochaetoides thermophila DSM 1495
G0SHF3 i.e. E1 subunit alpha, G0RYE0 i.e. E1 subunit beta
UniProt
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
Q0WQF7 i.e. dihydrolipoyllysine-residue acetyltransferase subunit 1 of pyruvate dehydrogenase complex, Q8RWN9 i.e. subunit 2 and Q5M729, i.e subunit 3, respectively, cf. EC 2.3.1.12
UniProt
brenda
Q8H1Y0 i.e. IAR4, E1 component subunit alpha-2, Q38799 i.e. PDH2, E1 component subunit beta-1, cf. EC 1.2.4.1
UniProt
brenda
-
-
-
brenda
subunit E1p, cf. EC 1.2.4.1
UniProt
brenda
-
94881, 94884, 94893, 348914, 348924, 348927, 348930, 348938, 348957, 672469, 759453 -
-
brenda
calf
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brenda
E1 component of the pyruvate dehydrogenase multienzyme complex
-
-
brenda
overview
-
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brenda
pyruvate dehydrogenase complex
-
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brenda
var. botrytis
-
-
brenda
var. italica, cauliflower, broccoli
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-
brenda
-
-
-
brenda
Q8NNF6 i.e. component E1, cf. EC 1.2.42, Q8NNJ2 i.e. component E2, cf. EC 2.3.1.61, Q8NTE1 i.e. component E3, cf. EC 1.8.1.4
UniProt
brenda
Q8NNF6 i.e. E1 component AceE, cf. EC 1.2.4.1
SwissProt
brenda
-
348914, 348915, 348921, 348932, 348933, 348934, 348943, 348953, 348956, 348966, 348967, 348976, 348982, 348991, 672520, 711033, 758772, 758903, 760075, 760205 -
-
brenda
Ace, E1 component, cf. EC 1.2.4.1
Uniprot
brenda
AceE, E1 component, cf. EC 1.2.4.1
Uniprot
brenda
E1 component AceE, cf. EC 1.2.4.1
Uniprot
brenda
E1 component, cf. EC 1.2.4.1
Uniprot
brenda
E3 component LpdA, cf. EC 1.8.1.4
UniProt
brenda
P06959 i.e. dihydrolipoyllysine-residue acetyltransferase component
UniProt
brenda
P06959 i.e. dihydrolipoyllysine-residue acetyltransferase component, cf. EC. 2.3.1.12
UniProt
brenda
P0AFG8 i.e. component E1/AceE, cf. EC 1.2.4.1, P06959 i.e. component E2/AceF, cf. EC 2.3.1.12, P0A9P0 i.e. component E3/LpdA, cf. EC 1.8.1.4
UniProt
brenda
P0AFG8 i.e. pyruvate dehydrogenase E1 component, cf. EC 1.2.4.1
Uniprot
brenda
-
-
-
brenda
enzyme is a component of the pyruvate dehydrogenase multienzyme complex
-
-
brenda
-
348920, 662948, 672520, 674601, 687353, 687748, 690088, 699383, 700076, 712786, 759549, 762550, 763312, 763321 -
-
brenda
comparison of recombinant somatic cell-specific isoform PDH1 and testis-specific isoform PDH2
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-
brenda
hyperdiploid strain of Ehrlich-Lettre ascites carcinoma cells
-
-
brenda
P08559 i.e. E1 component subunit alpha, P11177 i.e. E1 component subunit beta
UniProt
brenda
P08559 i.e. E1 component subunit alpha, Q86SW4 i.e. dihydrolipoamide acetyltransferase component
UniProt
brenda
P08559 i.e. pyruvate dehydrogenase E1 component subunit alpha, P11177 i.e. pyruvate dehydrogenase E1 component subunit beta
UniProt
brenda
P08559 i.e. subunit PdhA1, cf. EC 1.2.4.1, P11177 i.e. subunit PdhB1, cf. EC 1.2.4.1, O00330 i.e. subunit PdhX, P10515 i.e. subunit DlaT, cf. EC 2.3.1.12, P09622 i.e. subunit Dld, cf. EC 1.8.1.4, respectively
UniProt
brenda
P09622 i.e. E3 subunit, dihydrolipoyl dehydrogenase, cf. EC 1.8.1.4
UniProt
brenda
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-
-
brenda
E1 component subunit alpha
UniProt
brenda
P35486 i.e. E1 component subunit alpha, Q9D051 i.e. E1 component subunit beta
UniProt
brenda
-
-
-
brenda
dihydrolipoyllysine-residue acetyltransferase component, cf. EC 2.3.1.12
UniProt
brenda
-
-
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brenda
P52904 i.e. E1 component subunit beta, cf. EC 1.2.4.1, P52902 i.e. E1 component subunit alpha, cf. EC 1.2.4.1, P31023 i.e. dihydrolipoyl dehydrogenase, cf. EC 1.8.1.4
UniProt
brenda
P52904 i.e. E1 component subunit beta, P52902 i.e. E1 component subunit alpha
UniProt
brenda
pea
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brenda
-
-
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brenda
enzyme is in complex with alpha-ketoglutarate dehydrogenase
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brenda
-
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brenda
var. N5
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brenda
-
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brenda
E1 component subunit alpha
UniProt
brenda
Pda1, i.e. E1 component subunit alpha, cf. EC 1.2.4.1
UniProt
brenda
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-
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brenda
E1 component subunit alpha
UniProt
brenda
cv. romano
Uniprot
brenda
P52903 i.e. E1 component subunit alpha, P80503 i.e. dihydrolipoyl dehydrogenase, cf. EC 1.8.1.4
UniProt
brenda
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brenda
overview
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brenda
P74490 i.e. E1 component subunit alpha, P73405 i.e. E1 component subunit beta, cf. EC 1.2.4.1
UniProt
brenda
P74490 i.e. subunit PdhA, P73405 i.e. subunit PdhB, cf. EC 1.2.4.1
UniProt
brenda
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-
-
brenda
-
UniProt
brenda
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malfunction
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deletion of the E1a or E3 subunit genes of Plasmodium yoelii PDH causes no defect in blood stage development, mosquito stage development or early liver stage development. However, the gene deletions completely block the ability of the e1alpha- and e3-deficient parasites to form exo-erythrocytic merozoites during late liver stage development, thus preventing the initiation of a blood stage infection
physiological function
-
Plasmodium pyruvate dehydrogenase activity is only essential for the parasites progression from liver infection to blood infection. The sole role of PDH is to provide acetyl-CoA for FAS II. PDH subunits E1a and E3 subunits are not essential for either blood stage or mosquito stage development but are essential for late liver stage development
physiological function
-
pyruvate dehydrogenase is the rate-limiting enzyme coupling cytosolic glycolysis to mitochondrial citric acid cycle, and plays a critical role in maintaining homeostasis of brain glucose metabolism
physiological function
a hybrid complex consisting of E1p (thiamine diphosphate-dependent pyruvate dehydrogenase, AceE), E2 (dihydrolipoamide acetyltransferase, AceF), E3 (dihydrolipoamide dehydrogenase, Lpd), and E1o (thiamine diphosphate-dependent 2-oxoglutarate dehydrogenase, OdhA) contains six copies of E2 in its core. E2 forms a stable complex with E3 (E2-E3 subcomplex) in vitro, hypothetically comprised of two E2 trimers and four E3 dimers. E1o exists mainly as a hexamer in solution and is ready to form an active ODH complex when mixed with the E2-E3 subcomplex. In vitro, there is E1p- and E1o-dependent inhibition of ODH and PDH, respectively, actively supporting the formation of the hybrid complex, in which both E1p and E1o associate with a single E2-E3
physiological function
-
addition of excess pure E3 from Enterococcus faecalis may substitute for loss of Lactococcus lactis E3 during purification
physiological function
-
all the substrates, pyruvate, CoA and NAD+, exhibit cooperative klnetics towards the native enzyme complex. the calculated Hill coefficient for pyruvate is 1.34
physiological function
-
complete cross-reactivity is found with antibodies directed against the pyruvate dehydrogenase complex from Escherichia coli and electron micrographs of both enzyme complexes reveal identical structures
physiological function
-
dihydrolipoyl transacetylase subunit consists of 24 apparently identical polypeptide chains organized into a cube-like structure, and has the potential to bind 24 pyruvate dehydrogenase dimers in the absence of flavoprotein and 24 flavoprotein dimers in the absence of the pyruvate dehydrogenase subunit. The transacetylase can accommodate a total of only about 12 pyruvate dehydrogenase dimers and six flavoprotein dimers and this stoichiometry, which is the same as that of the native pyruvate dehydrogenase complex, produces maximum activity. Steric hindrance between the relatively bulky pyruvate dehydrogenase and flavoprotein molecules prevents the transacetylase from binding 24 molecules of each ligand
physiological function
disintegration of the pyruvate dehydrogenase complex core via double truncations (eight residues from E2 and seven residues from E3 binding protein PdhX) leads to the formation of highly active (approximately 70% of wild-type) unordered clusters or agglomerates and inactive nonagglomerated species (hexamer/trimer). After additional deletion of N-terminal swinging arms, the C-terminal truncations also cause the formation of agglomerates of minimized E2/E3 binding protein complexes
physiological function
-
in T37i murine preadipocytes differentiated into brown adipocytes, the flux through the TCA cycle is enhanced and regulated by pyruvate dehydrogenase (PDH) activity. PDH plays an important role in directing glucose carbons towards oxidation
physiological function
knockdown of the expression of the subunit 1 of the E2 dihydrolipoyllysine-residue acetyltransferase gene to 17 % of that in the wild-type has only a slight effect on plant growth whereas knockout of subunit 2 leads to an embryo-lethal phenotype. The nearly null mutation of subunit 3 does not cause any developmental abnormality
physiological function
mitochondrial proteins, Pkp2 (Ygl059wp) and Ppp2 (Ycr079wp), are engaged in the regulation of the pyruvate dehydrogenase complex by affecting the phosphorylation state of subunit Pda1. Ppp2 is almost exclusively localized in the mitochondrial matrix and associated with the complex. Cells lacking Ppp2 but also cells with a non-functional pyruvate dehydrogenase complex due to deletion of Pda1 possess similar sensitivity toward rapamycin
physiological function
residues in the lipoyl-lysine beta-turn region of the unlipoylated subunit E2p lipoyl domain undergo significant changes in both chemical shift and transverse relaxation time in the presence of subunit E1p but not E1o. Residue Gly11, in a prominent surface loop between beta-strands 1 and 2 in the E2p lipoyl domain, also undergoes a significant change in chemical shift. Addition of pyruvate to the mixture of unlipoylated E2p lipoyl domain and E1p causes larger changes in chemical shift and the appearance of multiple cross-peaks for certain residues. Residues in both beta-strands 4 and 5, together with those in the prominent surface loop and the following beta-strand 2, interact with E1p. The values of transverse relaxation time across the polypeptide chain backbone are lower than in the presence of E1p alone. The lipoylated domain E2p exhibits significant changes in chemical shift and decreases in the overall transverse relaxation times in the presence of E1p, the residues principally affected being restricted to the half of the domain that contains the lipoyl-lysine (Lys41) residue
physiological function
the active centers of the alpha2beta2 E1 component are not equivalent. In the activated active site, pyruvate is rapidly bound and decarboxylated with apparent forward rate constants of covalent pyruvate binding of 2 per s and decarboxylation of the formed 2-lactylthiamine intermediate of 5 per s. In the dormant site, these steps are as slow as 0.03 per s
physiological function
the activity of PDC is regulated by different isozymes of pyruvate dehydrogenase kinase PDK in different tissues. Isoform PDK1 is the principal isozyme regulating hepatic PDC. PDK2 is largely responsible for inactivation of PDC in tissues of muscle origin and brown adipose tissue (BAT). PDK3 is the principal kinase regulating pyruvate dehydrogenase activity in kidney and brain. In a well-fed state, the tissue levels of PDK4 protein are fairly low. In most tissues tested, PDK4 ablation has little effect on the overall rates of inactivation of PDC in kinase reaction
physiological function
the inner loop of the E1 component, i.e. residues 401-413, sequesters the active center from carboligase side reactions, assists the interaction between the E1 and the E2 components, thereby affecting the overall reaction rate of the entire multienzyme complex, and controls substrate access to the active center. Formation of the pre-decarboxylation intermediate is specifically affected by loop movement
physiological function
-
the time course for acetylation can be analyzed in terms of two kinetic processes. At long times 10 nmol of acetyl groups is incorporated per mg of enzyme complex. The slower process is much too slow to be of catalytic significance. The rate constant for the faster process is not dependent on enzyme concentration and reaches a limiting value of 40-65 per s at high pyruvate concentrations. The minimum molar turnover number of the enzyme complex is 420 per s (17.5 per s per pyruvate decarboxylase). The acetylated lipoic acids are deacetylated by coenzyme A at a rate much faster than that of acetylation. Complete deacetylation is obtained only if the deacetylation is carried out within seconds of the acetylation
physiological function
there are at least two loci of interaction between the E1 and E2 subunits: the thiamin diphosphate-bound substrate on E1 and the lipoylamide of E2, as reflected by the ability to reductively acetylate the latter and amino terminal residues 1-45 of E1 with regions of E2
physiological function
-
within the complex, the E1 enzyme pyruvate dehydrogenase (PDH) is the main regulatory site and is subject to inhibitory phosphorylation. Total PDH content does not change significantly during hibernation in any tissue but phospho-PDH content increases in all. Heart PDH shows increased phosphorylation at the three sites S232, S293, S300 by 8.1-, 10.6- and 2.1fold, respectively. Liver also shows elevated phospho-S300 (2.5fold) and phospho-S293 (4.7fold) content. Phosphorylation of S232 and S293 increases significantly in brain and lung but only S232 phosphorylation increases in kidney and skeletal muscle
physiological function
during lactate consumption, component E1 subunit alpha Ser293 and Ser300 phosphorylation levels are 33% higher compared to the phase of glucose excess. At the same time, the relative phosphorylation level of Ser232 increases steadily throughout the cultivation (66% increase overall). The intracellular pyruvate accumulates only during the period of high lactate production, while acetyl-CoA shows nearly no accumulation
physiological function
high salt intake downregulates sirtuin SIRT3 level in brown adipose tissue, accompanied by decreased oxygen consumption rate, and causes a severe loss of brown adipose tissue characteristics. SIRT3 interacts with pyruvate dehydrogenase E1alpha (PDHA1) and deacetylates residue Lys83 both in vitro and in vivo under high salt intake. In parallel, high salt intake suppresses salt-induced kinase (Sik) 2 phosphorylation. Silencing Sik2 further diminishes SIRT3 activity and enhances acetylation of PDHA1 K83. Reconstruction of SIRT3 restores PDH activity and thermogenic markers expression in differentiated brown adipocytes from SIRT3 knockout mice
physiological function
in Corynebacterium glutamicum, the PDH-ODH hybrid complex consists of six copies of subunit E2 in its core. E2 forms a stable complex with E3 (E2-E3 subcomplex) in vitro, hypothetically comprised of two E2 trimers and four E3 dimers. E1o exists mainly as a hexamer in solution and is ready to form an active ODH complex when mixed with the E2-E3 subcomplex. Inhibition of ODH and PDH is E1p- and E1o-dependent, respectively, actively supporting the formation Iof the hybrid complex, in which both E1p and E1o associate with a single E2-E3
physiological function
mitochondrial PDC E1 contributes to polar auxin transport during organ development. MAB1 encodes a mitochondrial PDC E1beta subunit that can form both a homodimer and a heterodimer with alpha-subunit IAR4. The MAB1 mutation impairs MAB1 homodimerization, reduces the abundance of IAR4 and IAR4L, weakens PDC enzymatic activity, and diminishes mitochondrial respiration. Mutation leads to significant changes in metabolites including amino acids, and an accumulation of Ala. In MAB1 mutants and seedlings where the TCA cycle is pharmacologically blocked, reduced abundance of the PIN-FORMED (PIN) auxin efflux carriers is found
physiological function
-
nitric oxide produced by murine macrophages is responsible for TCA cycle alterations and citrate accumulation associated with polarization. Inflammatory macrophages reroute pyruvate away from pyruvate dehydrogenase in an NO-dependent and hypoxia-inducible factor Hif1alpha-independent manner, thereby promoting glutamine-based anaplerosis
physiological function
the pyruvate dehydrogenase complex PDC displays size versatility in an ionic strength-dependent manner. Yeast PDC is a salt-labile complex that dissociates into submegadalton individual components even under physiological ionic strength. The ionic strength can modulate its catalytic activity
physiological function
-
in Corynebacterium glutamicum, the PDH-ODH hybrid complex consists of six copies of subunit E2 in its core. E2 forms a stable complex with E3 (E2-E3 subcomplex) in vitro, hypothetically comprised of two E2 trimers and four E3 dimers. E1o exists mainly as a hexamer in solution and is ready to form an active ODH complex when mixed with the E2-E3 subcomplex. Inhibition of ODH and PDH is E1p- and E1o-dependent, respectively, actively supporting the formation Iof the hybrid complex, in which both E1p and E1o associate with a single E2-E3
-
physiological function
-
the pyruvate dehydrogenase complex PDC displays size versatility in an ionic strength-dependent manner. Yeast PDC is a salt-labile complex that dissociates into submegadalton individual components even under physiological ionic strength. The ionic strength can modulate its catalytic activity
-
physiological function
-
a hybrid complex consisting of E1p (thiamine diphosphate-dependent pyruvate dehydrogenase, AceE), E2 (dihydrolipoamide acetyltransferase, AceF), E3 (dihydrolipoamide dehydrogenase, Lpd), and E1o (thiamine diphosphate-dependent 2-oxoglutarate dehydrogenase, OdhA) contains six copies of E2 in its core. E2 forms a stable complex with E3 (E2-E3 subcomplex) in vitro, hypothetically comprised of two E2 trimers and four E3 dimers. E1o exists mainly as a hexamer in solution and is ready to form an active ODH complex when mixed with the E2-E3 subcomplex. In vitro, there is E1p- and E1o-dependent inhibition of ODH and PDH, respectively, actively supporting the formation of the hybrid complex, in which both E1p and E1o associate with a single E2-E3
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1000000
and 2000000, gel filtration, enzyme isolated from mitochondria-enriched high sedimentation rate fraction
182000 - 183000
-
light scattering
190000
-
sedimentation equilibrium centrifugation
206000
-
scanning transmission electron microscopy
230000
gel filtration, mammalian E1p, mE1palpha (PDHA1) and mE1pbeta (PDHB1), and mE3 components are detected mostly in sub-megadalton size fractions of the high ionic strength fraction
230000 - 440000
gel filtration, enzyme isolated from nuclei-enriched low sedimentation rate fraction
40000
-
alpha2,beta2, 2 * 43000 + 2 * 40000, SDS-PAGE, immunoblotting
50000
-
60 * 41000 (E1 alpha) + 60 * 36000 (E1 beta) + 60 * 52000 (E2, EC 2.3.1.12) + 12 * 55000 (E3, EC 1.8.1.4) + 8-12 * 50000 (component X) + kinase and phosphatase components, heart pyruvate dehydrogenase complex
52000
-
60 * 41000 (E1 alpha) + 60 * 36000 (E1 beta) + 60 * 52000 (E2, EC 2.3.1.12) + 12 * 55000 (E3, EC 1.8.1.4) + 8-12 * 50000 (component X) + kinase and phosphatase components, heart pyruvate dehydrogenase complex
55000
-
60 * 41000 (E1 alpha) + 60 * 36000 (E1 beta) + 60 * 52000 (E2, EC 2.3.1.12) + 12 * 55000 (E3, EC 1.8.1.4) + 8-12 * 50000 (component X) + kinase and phosphatase components, heart pyruvate dehydrogenase complex
56000
-
alpha2,beta2, 2 * 38000 + 2 * 56000, SDS-PAGE, N-terminal amino acid sequencing
92500
-
x * 92500, SDS-PAGE
94000
-
2 * 94000, SDS-PAGE
99474
-
2 * 99474, calculation from nucleotide sequence
100000
-
sucrose density gradient centrifugation
100000
-
1 * 100000, SDS-PAGE
100000
-
x * 100000, SDS-PAGE
100000
-
2 * 100000, SDS-PAGE
2000000
and 1000000, gel filtration, enzyme isolated from mitochondria-enriched high sedimentation rate fraction
2000000
gel filtration, E2 component eluted only as a megadalton complex even in the high sedimentation rate fraction
35000
-
alpha2,beta2, 2 * 45000 + 2 * 35000, SDS-PAGE
35000
-
alpha2,beta2, 2 * 45000 + 2 * 35000, SDS-PAGE
35000
-
alpha2,beta2, 2 * 41000 + 2 * 35000, SDS-PAGE
36000
-
alpha2,beta2, 2 * 41000 + 2 * 36000
36000
-
alpha2,beta2, 2 * 42000 + 2 * 36000, SDS-PAGE, calculated from gene sequence
36000
-
60 * 41000 (E1 alpha) + 60 * 36000 (E1 beta) + 60 * 52000 (E2, EC 2.3.1.12) + 12 * 55000 (E3, EC 1.8.1.4) + 8-12 * 50000 (component X) + kinase and phosphatase components, heart pyruvate dehydrogenase complex
37000
Pigeon
-
alpha2,beta2, 2 * 42000 + 2 * 37000, SDS-PAGE
37000
alpha2,beta2, 1 * 43000 + 1 * 41000 + 2 * 37000, SDS-PAGE
37000
-
x * 40000-41000 + x * 37000
38000
-
alpha2,beta2, 2 * 42000 + 2 * 38000, SDS-PAGE
38000
-
alpha2,beta2, 2 * 38000 + 2 * 56000, SDS-PAGE, N-terminal amino acid sequencing
41000
-
alpha2,beta2, 2 * 41000 + 2 * 36000
41000
alpha2,beta2, 1 * 43000 + 1 * 41000 + 2 * 37000, SDS-PAGE
41000
-
alpha2,beta2, 2 * 41000 + 2 * 35000, SDS-PAGE
41000
-
60 * 41000 (E1 alpha) + 60 * 36000 (E1 beta) + 60 * 52000 (E2, EC 2.3.1.12) + 12 * 55000 (E3, EC 1.8.1.4) + 8-12 * 50000 (component X) + kinase and phosphatase components, heart pyruvate dehydrogenase complex
42000
-
alpha2,beta2, 2 * 42000 + 2 * 38000, SDS-PAGE
42000
Pigeon
-
alpha2,beta2, 2 * 42000 + 2 * 37000, SDS-PAGE
42000
-
alpha2,beta2, 2 * 42000 + 2 * 36000, SDS-PAGE, calculated from gene sequence
43000
alpha2,beta2, 1 * 43000 + 1 * 41000 + 2 * 37000, SDS-PAGE
43000
-
alpha2,beta2, 2 * 43000 + 2 * 40000, SDS-PAGE, immunoblotting
45000
-
alpha2,beta2, 2 * 45000 + 2 * 35000, SDS-PAGE
45000
-
alpha2,beta2, 2 * 45000 + 2 * 35000, SDS-PAGE
additional information
-
-
additional information
-
-
additional information
-
MW of native complex from heart: 740000 Da
additional information
-
MW of native complex isolated from kidney and heart: 7000000 Da and 8500000 Da respectively
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heterotetramer
-
x-ray crystallography
monomer
-
1 * 100000, SDS-PAGE
?
-
x * 40000-41000 + x * 37000
dimer
-
2 * 94000, SDS-PAGE
dimer
-
2 * 99474, calculation from nucleotide sequence
dimer
-
2 * 95000-96500, SDS-PAGE with and without urea
dimer
-
2 * 100000, SDS-PAGE
dimer
-
alpha2,beta2, 2 * 43000 + 2 * 40000, SDS-PAGE, immunoblotting
dimer
-
alpha2,beta2, 2 * 38000 + 2 * 56000, SDS-PAGE, N-terminal amino acid sequencing
multimer
-
x * 68000, lipoate acetyltransferase, x * 54800, lipoamide dehydrogenase, x *41900, alpha-pyruvate dehydrogenase, x * 45000, beta-pyruvate dehydrogenase subunit, plus x * 45000, component X, SDS-PAGE
multimer
-
x *42000 and x * 37000, alpha- and beta-subunits of pyruvate dehydrogenase, respectively, x * 76000, lipoate acetyltransferase, and x * 56000, lipoamide dehydrogenase. Two unknown polypeptides of 46000 and 41000 are additionally detected
multimer
-
x * 57000, x * 54000, x * 42000 and x * 36000, respectively, SDS-PAGE. The empirical unit must be repeated at least 50 times to make up the assembled complex
multimer
x * 70000, E2 subunit, x * 55000, E3 subunit, SDS-PAGE
multimer
-
x * 160000, x * 57600, x * 55600, x * 52500, x * 37100, SDS-PAGE
multimer
-
x * 100000, pyruvate dehydrogenase, x * 87000, dihydrolipoamide transacetylase (acetyl-CoA:dihydrolipoamide S-acetyltransferase, EC 2.3.1.12), and x * 56000, dihydrolipoamide dehydrogenase (NADH:lipoamide oxidoreductase, EC 1.6.4.3) components, respectively, SDS-PAGE
multimer
x * 78000, i.e. dihydrolipoamide transacetylase (E2) subunit, x * 60000, x * 58000, i.e. dihydrolipoamide dehydrogenase (E3) subunit, x * 55000, x * 43000 and x * 41000, i.e. alpha-subunits of pyruvate dehydrogenase, and x * 37000, i.e. beta-subunit of pyruvate dehydrogenase (E1), respectively, SDS-PAGE
multimer
-
x * 39800, x * 41700, 53700, and 57500, i.e. pyruvate decarboxylase subunits (E1), lipoate acetyltransferase (E2), and lipoamide dehydrogenase (E3), respectively, SDS-PAGE
oligomer
-
x * 58000-59000, i.e. transacetylase, x * 53 000, i.e. lipoamide dehydrogenase, x * 40000-41000, x * 37000, SDS-PAGE
oligomer
-
x * 58000-59000, i.e. transacetylase, x * 53 000, i.e. lipoamide dehydrogenase, x * 40000-41000, x * 37000, SDS-PAGE
-
oligomer
-
60 * 41000 (E1 alpha) + 60 * 36000 (E1 beta) + 60 * 52000 (E2, EC 2.3.1.12) + 12 * 55000 (E3, EC 1.8.1.4) + 8-12 * 50000 (component X) + kinase and phosphatase components, heart pyruvate dehydrogenase complex
oligomer
-
quaternary structure of pyruvate dehydrogenase complex
tetramer
-
alpha2,beta2, 2 * 42000 + 2 * 38000, SDS-PAGE
tetramer
-
alpha2,beta2, 2 * 41000 + 2 * 36000
tetramer
-
alpha2,beta2, 2 * 42000 + 2 * 36000, SDS-PAGE, calculated from gene sequence
tetramer
Pigeon
-
alpha2,beta2, 2 * 42000 + 2 * 37000, SDS-PAGE
tetramer
-
alpha2,beta2, 2 * 41000 + 2 * 35000, SDS-PAGE
tetramer
-
alpha2,beta2, 2 * 45000 + 2 * 35000, SDS-PAGE
tetramer
-
alpha2,beta2, 2 * 45000 + 2 * 35000, SDS-PAGE
tetramer
alpha2,beta2, 1 * 43000 + 1 * 41000 + 2 * 37000, SDS-PAGE
additional information
-
lipoamide dehydrogenase and two unknown polypeptides bind tightly to complex
additional information
-
enzyme component organization and binding structures in the pyruvate dehydrogenase multienzyme complex, core is formed by compoenents E2 and E3, regulatory role
additional information
-
identification of key amino acid residues responsible for enzyme component assembly to the multienzyme complex, overview
additional information
-
analysis of pyruvate dehydrogenase core complex consisting of dihydrolipoyl acetyltransferase and dihydrolipoyl dehydrogenase enzymes and comparison with structure of enzyme complex with dihydrolipoyl acetyltransferase
additional information
-
analysis of architecture of enzyme subunits in pyruvate dehydrogenase complex. Complex contains 30 enzyme heterotetramers plus dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase multimers
additional information
-
the affinity of PDH2 for the PDH-binding domain of E2 of pyruvate dehydrogenase complex differs only modestly from that of PDH1, surface plasma resonance studies
additional information
PDC displays size versatility in an ionic strength-dependent manner. PDC is a salt-labile complex that dissociates into sub-megadalton individual components even under physiological ionic strength. Each oligomeric component of PDC displays a larger size than expected. The activity of PDC is reduced in higher ionic strength
additional information
-
the complex consists of four subunits, i.e. E1alpha (44 kDa), E1beta (35 kDa), E2 (73 kDa), and E3 (60 kDa), SDS-PAGE
additional information
-
PDC displays size versatility in an ionic strength-dependent manner. PDC is a salt-labile complex that dissociates into sub-megadalton individual components even under physiological ionic strength. Each oligomeric component of PDC displays a larger size than expected. The activity of PDC is reduced in higher ionic strength
additional information
PDC displays size versatility in an ionic strength-dependent manner. PDC is a salt-labile complex that dissociates into sub-megadalton individual components even under physiological ionic strength. Each oligomeric component of PDC displays a larger size than expected. The activity of PDC is reduced in higher ionic strength
additional information
-
the pyruvate dehydrogenase complex PDC displays size versatility in an ionic strength-dependent manner. Yeast PDC is a salt-labile complex that dissociates into submegadalton individual components even under physiological ionic strength. The ionic strength can modulate its catalytic activity. E1 elutes at fractions for about 440 kDa proteins that mainly contain E1alpha, E1beta, and a nominal amount of E2. E3 elutes at fractions for about 230 kDa, which contain mostly E3
additional information
the pyruvate dehydrogenase complex PDC displays size versatility in an ionic strength-dependent manner. Yeast PDC is a salt-labile complex that dissociates into submegadalton individual components even under physiological ionic strength. The ionic strength can modulate its catalytic activity. E1 elutes at fractions for about 440 kDa proteins that mainly contain E1alpha, E1beta, and a nominal amount of E2. E3 elutes at fractions for about 230 kDa, which contain mostly E3
additional information
-
PDC displays size versatility in an ionic strength-dependent manner. PDC is a salt-labile complex that dissociates into sub-megadalton individual components even under physiological ionic strength. Each oligomeric component of PDC displays a larger size than expected. The activity of PDC is reduced in higher ionic strength
-
additional information
-
the pyruvate dehydrogenase complex PDC displays size versatility in an ionic strength-dependent manner. Yeast PDC is a salt-labile complex that dissociates into submegadalton individual components even under physiological ionic strength. The ionic strength can modulate its catalytic activity. E1 elutes at fractions for about 440 kDa proteins that mainly contain E1alpha, E1beta, and a nominal amount of E2. E3 elutes at fractions for about 230 kDa, which contain mostly E3
-
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D15A
variant is neither able to form a complex with the E2 component, nor to produce NADH in the overall assay
D7A
variant is neither able to form a complex with the E2 component, nor to produce NADH in the overall assay
D9A
variant is neither able to form a complex with the E2 component, nor to produce NADH in the overall assay
E12D
variant is neither able to form a complex with the E2 component, nor to produce NADH in the overall assay
E12Q
variant is neither able to form a complex with the E2 component, nor to produce NADH in the overall assay
E401A
mutant displays a modest threefold increase in Km pyruvate, and a significant reduction in kcat/Km pyruvate
H407A
mutation in E1, only modestly affects catalysis through the pyruvate decarboxylation step in isolated E1 (14% activity relative to parental E1), but inhibits the overall complex reaction by three orders of magnitude (0.15% activity compared to parental E1)
I11A
variant is able to form a complex with the E2 component, and produce NADH in the overall assay
I350V/A351V/A358V
PDH activity with the triple mutant at an [NADH]/[NAD+] ratio of 0.15 is higher than that of the wild-type without NADH addition. Within the PDH complex, the mutant is also less sensitive to inhibition by NADH
K403A
mutant displays a modest threefold increase in Km pyruvate, and a significant reduction in kcat/Km pyruvate
N404A
mutation leads to the greatest reduction in overall activity among the alanine-substituted variants and also greatly affects the Kd methyl acetylphosphonate
P10A
variant is able to form a complex with the E2 component, and produce NADH in the overall assay
R14A
variant is neither able to form a complex with the E2 component, nor to produce NADH in the overall assay
T13A
variant is able to form a complex with the E2 component, and produce NADH in the overall assay
Y177A
11% residual pyruvate dehydrogenase multienzyme complex activity, binding of thiamine diphosphate is unaffected
Y177F
7% residual pyruvate dehydrogenase multienzyme complex activity
M131A
-
mutation in the peripheral subunit-binding domain of the E2 chain. Residue M131 makes a significant contribution to the binding of pyruvate decarboxylase E1. Mutation lowers the binding affinity for pyruvate decarboxylase E1 by almost 140fold
R135A
-
mutation in the peripheral subunit-binding domain of the E2 chain, lowers the binding affinity for pyruvate decarboxylase E1 by almost 140fold
R135C
-
mutation in the peripheral subunit-binding domain of the E2 chain, plays an important part in the interaction with both pyruvate decarboxylase E1 and dihydrolipoyl dehydrogenase E3
R135K
-
mutant behaves almost like the wild-type
R156A
-
mutation in the peripheral subunit-binding domain of the E2 chain, lowers the binding affinity for pyruvate decarboxylase E1 by almost 19fold
D289A
-
the mutant does not have any detectable activity in PDC assay while its activity in thedecarboxylation reaction measured by 2,6-dichlorophenolindophenol assay does not significantly change
D289N
-
the mutant does not demonstrate any change in the 2,6-dichlorophenolindophenol assay but its activity is reduced to 67% in PDC assay
D413A
substitutions has no large effects on E3 activity when measured in its free form. However, when reconstituted in the complex, the pyruvate dehydrogenase activity is reduced to 18%. The binding affinities of the mutant to the the di-domain of the E3-binding protein are severely reduced
E229A
-
the mutant does not show any significant changes compared with the wild type subunit E1 activity
E229Q
-
the mutant does not show any significant changes compared with the wild type subunit E1 activity
E232A
-
the mutant does not show any significant changes compared with the wild type subunit E1 activity
E232Q
-
the mutant does not show any significant changes compared with the wild type subunit E1 activity
E234A
-
the mutant does not show any significant changes compared with the wild type subunit E1 activity
E234Q
-
the mutant does not show any significant changes compared with the wild type subunit E1 activity
H63A
-
about 17% residual activity in assay using 2,6-dichlorophenolindophenol, only modest inhibition by acetylphosphinate and acetylmethylphosphinate
I329A
-
the mutant shows reductions in activities in both the 2,6-dichlorophenolindophenol and PDC assays
I329del
-
the mutant shows reductions in activities in both the 2,6-dichlorophenolindophenol and PDC assays
M153V
-
the mutant shows decreased PDH activity in fibroblasts, around 30% of mean control
Q206L
-
the mutant shows decreased PDH activity in fibroblasts, around 52% of mean control
S203A
-
isoform PDH2, mutation of phosphorylation site
S203A/S271A
-
phosphorylation at remaining site S264 causes 96% inactivation
S203A/S64A
-
phosphorylation at remaining site S271 causes complete inactivation
S203E
-
isoform PDH2, mutation of phosphorylation site
S264A
-
isoform PDH2, mutation of phosphorylation site, no enzymic activity
S264E
-
isoform PDH2, mutation of phosphorylation site
S271A
-
isoform PDH2, mutation of phosphorylation site, no enzymic activity
S271E
-
isoform PDH2, mutation of phosphorylation site
S64A/S271A
-
phosphorylation at remaining site S203 causes 91% inactivation
Y438A
substitutions has no large effects on E3 activity when measured in its free form. However, when reconstituted in the complex, the pyruvate dehydrogenase activity is reduced to 9%. The binding affinities of the mutant to the the di-domain of the E3-binding protein are severely reduced and binding of is accompanied by an unfavorable enthalpy change and a large positive entropy change
Y438H
substitutions has no large effects on E3 activity when measured in its free form. However, when reconstituted in the complex, the pyruvate dehydrogenase activity is reduced to 20%. The binding affinities of the mutant to the the di-domain of the E3-binding protein are severely reduced
additional information
construction of a cysteine-less variant of the E1 component, onto which cysteines are substituted at selected loop positions. In the absence of ligand, the loop exists in two conformations, and the rate constant for loop movement is of the same order of magnitude as the turnover number for the enzyme under the same conditions
additional information
construction of deletion mutants of the E1 pyruvate dehydrogenase component lacking amino acids 6-15, 16-25, 26-35, 36-45, and 46-55, along with single-site substitutions at Asp7, Asp9, Pro10, Ile11, Glu12, Thr13, Arg14, and Asp15. The decarboxylation of pyruvate and the ability of PDHc-E1 to dimerize are not affected by any of the deletions or substitutions. Deletion mutant 46-55 and the Pro10Ala, Ile11Ala, and Thr13Ala variants are able to form a complex with the E2 component, and produce NADH in the overall assay, deletion mutants 16-25, 26-35, and 36-45 and the Asp7Ala, Asp9Ala, Glu12Gln, Glu12Asp, Arg14Ala, and Asp15Ala variants fail in both. All constructs can carry out reductive acetylation of the Escherichia coli lipoyl domain and reductively acetylate the Escherichia coli E2 component
additional information
mutation of a prominent surface loop that links the first and second beta-strands in all lipoyl domains, of E2 dihydrolipoyl acetyltransferase. Deletion of the loop (four residues) renders the domain incapable of reductive acetylation by pyruvate dehydrogenase complex subunit E1p in the presence of pyruvate. Additional exchange of the two residues on the C-terminal side of the loop (V14A, E15T) has no effect. Exchanging the residue on the N-terminal side of the lipoyl-lysine beta-turn in the E2p and E2o domains (G39T), both singly and in conjunction with the loop exchange, has no effect on the ability of the E2p domain to be reductively acetylated but does confer a slight increase in susceptibility to reductive succinylation. All mutant E2p domains, apart from that with the loop deletion, are readily lipoylated in vitro by lipoate protein ligase A
additional information
-
mutational analysis of key amino acid residues responsible for enzyme component assembly to the multienzyme complex using E3 component mutants, overview
additional information
-
residues K136, K153, R146, S133 do not contribute to the interaction with pyruvate decarboxylase E1
additional information
-
the in-frame deletion mutant G143del and the 65 bp duplication mutant c.900-6_958dup65 show decreased PDH activity in fibroblasts, around 16% of mean control
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alpha and beta subunits purified from enzyme complex after gel filtration in the presence of 2 M KI followed by chromatography on hydroxyapatite in the presence of 8 M urea
-
isolation of EC 1.2.4.1 after elastase treatment of the complex and gel filtration
-
Ni2+-Sepharose column chromatography
-
purification of pyruvate dehydrogenase complex including pyruvate decarboxylase E1
-
purification procedure for the 2-oxoglutarate dehydrogenase and the pyruvate dehydrogenase complexes from mitochondria. After fractionated precipitations with polyethylene glycol, elimination of thiol proteins, and gel-filtration chromatography, the resulting preparations contain both activities. Covalent chromatography on thiol-activated Sepharose CL-4B allows the specific binding of the 2-oxoglutarate dehydrogenase complex activity in the presence of 2-oxoglutarate, the pyruvate dehydrogenase complex activity is retained in the presence of pyruvate
-
purification scheme for the pyruvate dehydrogenase complex directly from body wall muscle which yields a fully activated pyruvate dehydrogenase complex with substantial PDHa kinase activity
-
pyruvate dehydrogenase can be resolved from complex by incubation with 8 M urea, 4 M guanidinium chloride, 100 mM glycine/NaOH, pH 9.0 followed by gel filtration
-
pyruvate dehydrogenase complex composed of EC 1.2. 4.1, EC 2.3.1.12, EC 1.8.1.4
Pigeon
-
pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
pyruvate dehydrogenase complex from ox heart, by PEG fractionation, ultracentrifugation, and gel filtration
-
pyruvate dehydrogenase complex, composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
pyruvate dehydrogenase purified from complex by gel filtration
-
recombinant multienzyme complex components from Escherichia coli strain BL21(DE3) to homogeneity
-
The enzyme complex is resolved into its constituent proteins by means of gel filtration on Sepharose CL-6B in the presence of 2 M-KI, followed by chromatography on hydroxyapatite in the presence of 8 M urea. These harsh conditions are necessary to cause suitable dissociation of the enzyme complex
-
-
-
pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
-
pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
-
pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
-
pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
-
pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
-
pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
-
pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
-
pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
-
pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
-
pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
-
pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
-
pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
-
pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
-
pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
-
pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
-
pyruvate dehydrogenase complex, composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
Hansenula miso
-
pyruvate dehydrogenase complex, composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
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analysis
-
sensitive and rapid assay procedures for human mitochondrial the pyruvate dehydrogenase (PDH) complex, the 2-oxoglutarate dehydrogenase (OGDH) complex and their 5 component enzymes, for use with crude tissue extracts
medicine
-
enzyme/pyruvate dehydrogenase kinase dependent pathway is repressed in 73% of non-small cell lung carcinomas, which may be a key reason for hypoxia-inducible factor 1alpha stabilization and aerobic glycolysis. About half of enzyme-deficient carcinomas are not able to switch on the hypoxia-inducible factor 1alpha pathway, patients with these tumours have an excellent postoperative outcome. In contrast to cancer cells, fibroblasts in the tumour-supporting stroma exhibit an intense enzyme but reduced pyruvate dehydrogenase kinase 1 expression favoring maximum enzyme activity
medicine
in a patient with primary lactic acidaemia, about 30% residual pyruvate dehydrogenase activity is observed, while the Km value is similiar to control. The enzyme deficiency is likely to be quantitative rather than qualitative. The patient developed severe metabolic acidosis at 8 months, accompanied by elevation of serum lactate and pyruvate. The lactate and pyruvate concentrations are also increased in cerevbrospinal fluid
medicine
the acute promyelocytic leukemia is greatly alleviated in the PDT-PAO-F16 treated group in an acute promyelocytic leukemia mice model
medicine
high salt intake downregulates sirtuin SIRT3 level in brown adipose tissue, accompanied by decreased oxygen consumption rate, and causes a severe loss of brown adipose tissue characteristics. SIRT3 interacts with pyruvate dehydrogenase E1alpha (PDHA1) and deacetylates residue Lys83 both in vitro and in vivo under high salt intake. In parallel, high salt intake suppresses salt-induced kinase (Sik) 2 phosphorylation. Silencing Sik2 further diminishes SIRT3 activity and enhances acetylation of PDHA1 K83. Reconstruction of SIRT3 restores PDH activity and thermogenic markers expression in differentiated brown adipocytes from SIRT3 knockout mice
medicine
-
nitric oxide produced by murine macrophages is responsible for TCA cycle alterations and citrate accumulation associated with polarization. Inflammatory macrophages reroute pyruvate away from pyruvate dehydrogenase in an NO-dependent and hypoxia-inducible factor Hif1alpha-independent manner, thereby promoting glutamine-based anaplerosis
synthesis
expression of pyruvate decarboxylase and alcohol dehydrogenase in Clostridium thermocellum DSM 1313. Though both enzymes are functional in Clostridium thermocellum, the presence of alcohol dehydrogenase severely limits the growth of the recombinant strains, irrespective of the presence or absence of the pyruvate decarboxylase gene. The recombinant strain expressing pyruvate decarboxylase shows two-fold increase in pyruvate carboxylase activity and ethanol production when compared with the wild type strain
synthesis
-
metabolic engineering of Geobacillus thermoglucosidasius to divert the fermentative carbon flux from a mixed acid pathway to one in which ethanol becomes the major product, involving elimination of the lactate dehydrogenase and pyruvate formate lyase pathways by disruption of the ldh and pflB genes, respectively, and upregulation of expression of pyruvate dehydrogenase. Pyruvate dehydrogenase is active under anaerobic conditions, but expressed suboptimally for a role as the primary fermentation pathway. Strains with all three modifications form ethanol efficiently and rapidly at temperatures in excess of 60°C in yields in excess of 90% of theoretical. The strains also efficiently ferment cellobiose and a mixed hexose and pentose feed
synthesis
coexpression of pyruvate dehydrogenase (PDH) E1 alpha and E1 beta subunits in Escherichia coli leads to fully active E1 protein. The production of E1 alpha alone results in a catalytically inactive protein. The PDH E1 protein produced in Escherichia coli is capable of being phosphorylated by PDH-specific kinase
synthesis
exchange of the native Corynebacterium glutamicum promoter of the AceE gene, with mutated DapA promoter variants leads to a series of strains with gradually reduced growth rates and pyruvate dehydrogenase complex activities. Upon overexpression of the L-valine biosynthetic genes IlvBNCE, all strains produce L-valine. Additional deletion of the Pqo and Ppc genes, encoding pyruvate:quinone oxidoreductase and phosphoenolpyruvate carboxylase enables production of up to 738mM (i.e., 86.5 g/liter). Inactivation of the transaminase B gene (IlvE) and overexpression of IlvBNCD instead of ilvBNCE transform the L-valine-producing strain into a 2-ketoisovalerate producer, excreting up to 303mM (35 g/liter) 2-ketoisovalerate. The replacement of the AceE promoter by the DapA-A16 promoter improves the production by 100% and 44%, respectively
synthesis
production of the functional pyruvate dehydrogenase complex. All components are coexpressed in the cytoplasm of baculovirus-infected SF9 cells by deletion of the mitochondrial localization signal sequences and E1a is FLAG-tagged to facilitate purification. The protein complex is purified using FLAG-M2 affinity resin, followed by Superdex 200 sizing chromatography. The E2 and E3BP components are then lipoylated in vitro. The resulting complex is over 90% pure and homogenous
synthesis
-
metabolic engineering of Geobacillus thermoglucosidasius to divert the fermentative carbon flux from a mixed acid pathway to one in which ethanol becomes the major product, involving elimination of the lactate dehydrogenase and pyruvate formate lyase pathways by disruption of the ldh and pflB genes, respectively, and upregulation of expression of pyruvate dehydrogenase. Pyruvate dehydrogenase is active under anaerobic conditions, but expressed suboptimally for a role as the primary fermentation pathway. Strains with all three modifications form ethanol efficiently and rapidly at temperatures in excess of 60°C in yields in excess of 90% of theoretical. The strains also efficiently ferment cellobiose and a mixed hexose and pentose feed
-