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pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
pyruvate + CoA + oxidized 2,6-dichlorophenolindophenol
acetyl-CoA + CO2 + reduced 2,6-dichlorophenolindophenol
-
-
-
?
acetaldehyde + benzaldehyde
(R)-phenylacetylcarbinol
-
-
-
-
?
alpha-ketobutyrate + Fe(CN)63- + H2O
hydroxyacetate + CO2 + Fe(CN)64-
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
-
?
pyruvate + CoA + oxidized 2,6-dichlorophenolindophenol
acetyl-CoA + CO2 + reduced 2,6-dichlorophenolindophenol
pyruvate + E2p lipoyl domain
acetylated E2p lipoyl domain + CO2
-
-
-
-
?
pyruvate + Fe(CN)63- + H2O
CO2 + Fe(CN)64-
-
-
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
pyruvate + pyruvate dehydrogenase complex subunit E2p
?
-
-
-
-
?
pyruvate + [dihydrolipoyllysine-residue acetyltransferase]-lipoyllysine
[dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2
-
-
-
-
?
additional information
?
-
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
enzyme E1 is a component of the pyruvate dehydrogenase multienzyme complex PDHc, and catalyzes the first step of the multistep process
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
reaction of the citric acid or Krebs cycle
-
-
?
pyruvate + CoA + oxidized 2,6-dichlorophenolindophenol
acetyl-CoA + CO2 + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
pyruvate + CoA + oxidized 2,6-dichlorophenolindophenol
acetyl-CoA + CO2 + reduced 2,6-dichlorophenolindophenol
-
artificial electron acceptor
-
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
-
-
-
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
-
in overall reaction of pyruvate dehydrogenase complex, pyruvate can be replaced by 2-ketobutyrate
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
-
additional reactions of complex, e. g. reduction of K3Fe(CN)6
-
?
additional information
?
-
reactions performed by the whole enzyme complex, overview
-
-
?
additional information
?
-
-
reactions performed by the whole enzyme complex, overview
-
-
?
additional information
?
-
-
overall reaction of the multienzyme complex, overview
-
-
?
additional information
?
-
-
N-terminal residues 1-45 of the pyruvate dehydrogenase complex E1 subunit interact with the E2 subunit and are required for activity of the complex but not for reductive acetylation of the E2 subunit
-
-
?
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(2-chlorophenyl)(dimethoxyphosphoryl)methyl [3-(trifluoromethyl)phenoxy]acetate
-
(3,4-dichlorophenyl)(dimethoxyphosphoryl)methyl [3-(trifluoromethyl)phenoxy]acetate
-
(3-chlorophenyl)(dimethoxyphosphoryl)methyl [3-(trifluoromethyl)phenoxy]acetate
-
(4-chlorophenyl)(dimethoxyphosphoryl)methyl [3-(trifluoromethyl)phenoxy]acetate
-
(dimethoxyphosphoryl)(4-methylphenyl)methyl [3-(trifluoromethyl)phenoxy]acetate
-
(dimethoxyphosphoryl)(phenyl)methyl (2,3-dichlorophenoxy)acetate
-
(dimethoxyphosphoryl)(phenyl)methyl (2,6-dichlorophenoxy)acetate
-
(dimethoxyphosphoryl)(phenyl)methyl (2-chloro-5-methylphenoxy)acetate
-
(dimethoxyphosphoryl)(phenyl)methyl (3-fluorophenoxy)acetate
-
(dimethoxyphosphoryl)(phenyl)methyl (4-chloro-2-methylphenoxy)acetate
-
(dimethoxyphosphoryl)(phenyl)methyl (4-chloro-3-methylphenoxy)acetate
-
(dimethoxyphosphoryl)(phenyl)methyl (4-chlorophenoxy)acetate
-
(dimethoxyphosphoryl)(phenyl)methyl (4-fluorophenoxy)acetate
-
1-(dimethoxyphosphoryl)ethyl (2,3-dichlorophenoxy)acetate
-
1-(dimethoxyphosphoryl)ethyl (2,6-dichlorophenoxy)acetate
-
1-(dimethoxyphosphoryl)ethyl (2-chloro-5-methylphenoxy)acetate
-
1-(dimethoxyphosphoryl)ethyl (3-fluorophenoxy)acetate
-
1-(dimethoxyphosphoryl)ethyl (4-chloro-2-methylphenoxy)acetate
-
1-(dimethoxyphosphoryl)ethyl (4-chloro-3-methylphenoxy)acetate
-
1-(dimethoxyphosphoryl)ethyl (4-chlorophenoxy)acetate
-
1-(dimethoxyphosphoryl)ethyl (4-fluorophenoxy)acetate
-
2,2,2-trichloro-1-(dimethoxyphosphoryl)ethyl (2,3-dichlorophenoxy)acetate
-
2,2,2-trichloro-1-(dimethoxyphosphoryl)ethyl (2-chloro-5-methylphenoxy)acetate
-
2,2,2-trichloro-1-(dimethoxyphosphoryl)ethyl (3-fluorophenoxy)acetate
-
2,2,2-trichloro-1-(dimethoxyphosphoryl)ethyl (4-chloro-2-methylphenoxy)acetate
-
2,2,2-trichloro-1-(dimethoxyphosphoryl)ethyl (4-chloro-3-methylphenoxy)acetate
-
2,2,2-trichloro-1-(dimethoxyphosphoryl)ethyl (4-chlorophenoxy)acetate
-
2,2,2-trichloro-1-(dimethoxyphosphoryl)ethyl (4-fluorophenoxy)acetate
-
5-((4-((4-chlorophenoxy)methyl)-5-iodo-1H-1,2,3-triazol-1-yl)methyl)-2-methylpyrimidin-4-amine
formation of intermolecular hydrogen bonding and halogen bonding. The 5-iodo-1,2,3-triazole and benzene ring play important roles in the biological activities of the compound. The iodine atom may participate in the halogen bonding with the negatively charged and can form a halogen bonding with the O atom of Asp521 in the active site of PDH-E1
O,O-dimethyl (2,3-dichlorophenoxyacetoxy)(furan-2-yl)-methylphosphonate
-
O,O-dimethyl (2,3-dichlorophenoxyacetoxy)(thien-2-yl)-methylphosphonate
-
O,O-dimethyl (2,4-dichlorophenoxyacetoxy)(furan-2-yl)-methylphosphonate
-
O,O-dimethyl (2,4-dichlorophenoxyacetoxy)(thien-2-yl)-methylphosphonate
-
O,O-dimethyl (2,6-dichlorophenoxyacetoxy)(furan-2-yl)-methylphosphonate
-
O,O-dimethyl (2,6-dichlorophenoxyacetoxy)(thien-2-yl)-methylphosphonate
-
O,O-dimethyl (2-chloro-5-methylphenoxyacetoxy)(furan-2-yl)methylphosphonate
-
O,O-dimethyl (2-chloro-5-methylphenoxyacetoxy)(thien-2-yl)methylphosphonate
-
O,O-dimethyl (3-fluorophenoxyacetoxy)(furan-2-yl)methylphosphonate
-
O,O-dimethyl (3-fluorophenoxyacetoxy)(thien-2-yl)methylphosphonate
-
O,O-dimethyl (4-chloro-2-methylphenoxyacetoxy)(furan-2-yl)methylphosphonate
-
O,O-dimethyl (4-chloro-2-methylphenoxyacetoxy)(thien-2-yl)methylphosphonate
-
O,O-dimethyl (4-chloro-3-methylphenoxyacetoxy)(furan-2-yl)methylphosphonate
-
O,O-dimethyl (4-chloro-3-methylphenoxyacetoxy)(thien-2-yl)methylphosphonate
-
O,O-dimethyl (4-chlorophenoxyacetoxy)(furan-2-yl)methylphosphonate
-
O,O-dimethyl (4-chlorophenoxyacetoxy)(thien-2-yl)methylphosphonate
-
O,O-dimethyl (4-fluorophenoxyacetoxy)(furan-2-yl)methylphosphonate
-
sodium methyl [[[(2,4-dichlorophenoxy)acetyl]oxy](2,4-dichlorophenyl)methyl]phosphonate
-
sodium methyl [[[(2,4-dichlorophenoxy)acetyl]oxy](3-nitrophenyl)methyl]phosphonate
-
sodium methyl [[[(2,4-dichlorophenoxy)acetyl]oxy](4-fluorophenyl)methyl]phosphonate
-
sodium methyl [[[(2,4-dichlorophenoxy)acetyl]oxy](4-methoxyphenyl)methyl]phosphonate
-
sodium methyl [[[(2,4-dichlorophenoxy)acetyl]oxy](phenyl)methyl]phosphonate
-
sodium o-methyl (2,4-dichlorophenoxyacetoxy)(2-chlorophenyl)methylphosphonate
-
sodium o-methyl (2,4-dichlorophenoxyacetoxy)(3,4-dichlorophenyl)methyl phosphonate
-
sodium o-methyl (2,4-dichlorophenoxyacetoxy)(4-chlorophenyl)methylphosphonate
-
sodium o-methyl (2,4-dichlorophenoxyacetoxy)(4-methylphenyl)methylphosphonate
-
sodium o-methyl (2,4-dichlorophenoxyacetoxy)(furan-2-yl)methylphosphonate
-
sodium o-methyl (2,4-dichlorophenoxyacetoxy)(pyridin-2-yl)methylphosphonate
-
thiamine 2-thiazolone diphosphate
crystallization data of complex with enzyme
thiamine thiazolone diphosphate
inhibits potently the E1 component of the pyruvate dehydrogenase multienzyme complex PDHc, competitive to cofactor thiamine diphosphate, binding structure and determinants, binding induced reorganisation of the active site conformation, mechanism, K392 is important, overview
3-Bromopyruvate
-
suicide substrate
4-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-5-iodo-1H-1,2,3-triazol-4-yl)methoxy)benzonitrile
-
exhibits very good enzyme-selective inhibition of PDH-E1 between pig heart and Escherichia coli and activity against Rhizoctonia solani and Botrytis cinerea even at 12.5 lg/ml
5-((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
Fluoropyruvate
-
competitive with respect to pyruvate, both free and complex bound enzyme behave in the same manner
Methylacetylphosphonate
-
-
NaBH4
-
rapid inactivation in the presence of thiamine diphosphate, may reduce thiamine diphosphate to produce a reversible inhibitor
Tetrahydrothiamine diphosphate
-
cis-isomer, 0.0013 mM, 50% inhibition
thiamine 2-thiothiazolone diphosphate
-
-
thiamine thiazolone diphosphate
-
-
thiamine thiothiazolone diphosphate
-
-
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0.08 - 95
E2p lipoyl domain
-
0.081
pyruvate
mutant enzyme H407A, with 2,6-dichlorophenolindophenol, at 30°C
0.21
pyruvate
mutant enzyme K403E, with 2,6-dichlorophenolindophenol, at 30°C
0.39
pyruvate
mutant enzyme E401K, with 2,6-dichlorophenolindophenol, at 30°C
1.53
pyruvate
mutant enzyme K410E, with 2,6-dichlorophenolindophenol, at 30°C
3.07
pyruvate
mutant enzyme N404A, with 2,6-dichlorophenolindophenol, at 30°C
3.64
pyruvate
mutant enzyme E401A, with 2,6-dichlorophenolindophenol, at 30°C
4.41
pyruvate
mutant enzyme K403A, with 2,6-dichlorophenolindophenol, at 30°C
7.68
pyruvate
mutant enzyme K410A, with 2,6-dichlorophenolindophenol, at 30°C
19.03
pyruvate
mutant enzyme Q408A, with 2,6-dichlorophenolindophenol, at 30°C
25.12
pyruvate
mutant enzyme K411E, with 2,6-dichlorophenolindophenol, at 30°C
35.13
pyruvate
mutant enzyme K411A, with 2,6-dichlorophenolindophenol, at 30°C
37.9
pyruvate
wild type enzyme, with 2,6-dichlorophenolindophenol, at 30°C
0.08
E2p lipoyl domain
-
mutant enzyme H407A, at pH 7.0 and 30°C
-
0.7
E2p lipoyl domain
-
mutant enzyme D549A, at pH 7.0 and 30°C
-
0.83
E2p lipoyl domain
-
mutant enzyme E401K, at pH 7.0 and 30°C
-
3.31
E2p lipoyl domain
-
mutant enzyme Y177A, at pH 7.0 and 30°C
-
95
E2p lipoyl domain
-
wild type enzyme, at pH 7.0 and 30°C
-
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in complex with phosphonolactylthiamine diphosphate as structural and electrostatic analogue of alpha-lactylthiamin diphosphate. Presence of phosphonolactylthiamin diphosphate causes large conformational changes
preparation of catalytic subunit E1 of pyruvate dehydrogenase complex, without cofactors thiamine diphosphate and Mg2+, no evidence of disorder/order loop transformations. Comparison with holo-E1 enzyme and in an inhibitor complex with thiamine 2-thiazolone diphosphate
purified enzyme E1 in complex with inhibitor thiamine thiazolone diphosphate and Mg2+, sitting drop vapour diffusion method, reservoir solution: 15-20% PEG 2000 monomethyl ether, 5-10% 2-propanol, 0.2% NaN3, 100 mM HEPES, pH 7.00, 22°C, 4 weeks, X-ray diffraction structure determination and analysis at 2.09 A resolution, comparison with structure determined with bound cofactor thiamine diphosphate
purified recombinant pyruvate dehydrogenase multienzyme complex component E1, sitting drop vapor diffusion method, mixing of equal amounts of protein and precipitant solution of 0.006-0.01 ml, the latter containing 15-20% PEG2000 monomethyl ether, 10% propanol, 0.2% NaN3, and 60 mM HEPES, pH 7.1, 22°C, 2-5 weeks, native and selenomethionine crystals, X-ray diffraction structure determination and analysis at 1.85 A resolution
sitting drop vapour diffusion method with 15-20% PEG2000 monomethyl ether, 10% propanol, 0.2% NaN3 in 60 mM HEPES buffer (pH 7.05)
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E401A
9.56% of overall wild type activity and 23.4% of wild type activity with 2,6-dichloroindolphenol
E401K
1.04% of overall wild type activity and 4.63% of wild type activity with 2,6-dichloroindolphenol
K403A
11.6% of overall wild type activity and 98.0% of wild type activity with 2,6-dichloroindolphenol
K403E
0.56% of overall wild type activity and 5.46% of wild type activity with 2,6-dichloroindolphenol
K410A
23.0% of overall wild type activity and 31.6% of wild type activity with 2,6-dichloroindolphenol
K410E
3.7% of overall wild type activity and 26.1% of wild type activity with 2,6-dichloroindolphenol
K411A
68.2% of overall wild type activity and 77.5% of wild type activity with 2,6-dichloroindolphenol
K411E
38.0% of overall wild type activity and 88.0% of wild type activity with 2,6-dichloroindolphenol
N404A
1.81% of overall wild type activity and 45.1% of wild type activity with 2,6-dichloroindolphenol
Q408A
31.5% of overall wild type activity and 112.1% of wild type activity with 2,6-dichloroindolphenol
D15A
-
site-directed mutagenesis, 0.19% remaining activity with NAD+ and 16% reduced E1 activity with 2,6-dichlorophenolindophenol as electron acceptor compared to the wild-type E1
D549A
-
in the mutant, binding and reductive acetylation of E2p lipoyl domains are highly impaired
D7A
-
site-directed mutagenesis, 0.14% remaining activity with NAD+ and 63% reduced E1 activity with 2,6-dichlorophenolindophenol as electron acceptor compared to the wild-type E1
D9A
-
site-directed mutagenesis, inactive with NAD+, 80% reduced E1 activity with 2,6-dichlorophenolindophenol as electron acceptor compared to the wild-type E1
E12D
-
site-directed mutagenesis, 2.3% remaining activity with NAD+ and 90% reduced E1 activity with 2,6-dichlorophenolindophenol as electron acceptor compared to the wild-type E1
E12Q
-
site-directed mutagenesis, 3.3% remaining activity with NAD+ and 59% reduced E1 activity with 2,6-dichlorophenolindophenol as electron acceptor compared to the wild-type E1
E401K
-
in the mutant, binding and reductive acetylation of E2p lipoyl domains are highly impaired
E410K
-
CC-bond formation is dramatically slowed down (10-fold compared with E1ec) in E401K, the loop dynamics apparently greatly influences covalent addition of substrate to the enzyme-bound thiamine diphosphate
H407A
-
in the mutant, binding and reductive acetylation of E2p lipoyl domains are highly impaired
I11A
-
site-directed mutagenesis, 94% remaining activity with NAD+ and E1 activity with 2,6-dichlorophenolindophenol as electron acceptor is like the wild-type E1 activity
P10A
-
site-directed mutagenesis, unaltered activity with NAD+ and 50% reduced E1 activity with 2,6-dichlorophenolindophenol as electron acceptor compared to the wild-type E1
R14A
-
site-directed mutagenesis, 0.25% remaining activity with NAD+ as electron acceptor, E1 activity with 2,6-dichlorophenolindophenol is like the wild-type E1 activity
T13A
-
site-directed mutagenesis, 13% remaining activity with NAD+ and 26% reduced E1 activity with 2,6-dichlorophenolindophenol as electron acceptor compared to the wild-type E1
Y177F
-
7% of wild-type activity in enzyme complex
additional information
-
construction of several N-terminal E1 deletion mutants by tryptic or chymotryptic digest all showing reduced enzyme activity
H407A
crystallization data. Interaction between H407 and phosphonolactylthiamine diphosphate is essential for stabilization of two loop regions in the active site
H407A
0.15% of overall wild type activity and 12.0% of wild type activity with 2,6-dichloroindolphenol
Y177A
-
11% of wild-type activity in enzyme complex
Y177A
-
in the mutant, binding and reductive acetylation of E2p lipoyl domains are highly impaired
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Apfel, M.A.; Ikeda, B.H.; Speckhard, D.C.; Frey, P.A.
Escherichia coli pyruvate dehydrogenase complex. Thiamin pyrophosphate-dependent inactivation by 3-bromopyruvate
J. Biol. Chem.
259
2905-2909
1984
Escherichia coli
brenda
Lowe, P.N.; Leeper, F.J.; Perham, R.N.
Stereoisomers of tetrahydrothiamin pyrophosphate, potent inhibitors of the pyruvate dehydrogenase multienzyme complex from Escherichia coli
Biochemistry
22
150-157
1983
Escherichia coli
brenda
Saumweber, H.; Binder, R.; Bisswanger, H.
Pyruvate dehydrogenase component of the pyruvate dehydrogenase complex from Escherichia coli K12. Purification and characterization
Eur. J. Biochem.
114
407-411
1981
Escherichia coli
brenda
Reed, L.J.; Willms, C.R.
Purification and resolution of the pyruvate dehydrogenase complex (Escherichia coli)
Methods Enzymol.
9
247-265
1966
Escherichia coli
-
brenda
Nemeria, N.; Yan, Y.; Zhang, Z.; Brown, A.M.; Arjunan, P.; Furey, W.; Guest, J.R.; Jordan, F.
Inhibition of the Escherichia coli pyruvate dehydrogenase complex E1 subunit and its tyrosine 177 variants by thiamin 2-thiazolone and thiamin 2-thiothiazolone diphosphates. Evidence for reversible tight-binding inhibition
J. Biol. Chem.
276
45969-45978
2001
Escherichia coli, Homo sapiens
brenda
Arjunan, P.; Nemeria, N.; Brunskill, A.; Chandrasekhar, K.; Sax, M.; Yan, Y.; Jordan, F.; Guest, J.R.; Furey, W.
Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution
Biochemistry
41
5213-5221
2002
Escherichia coli (P0AFG8), Escherichia coli
brenda
Park, Y.H.; Wei, W.; Zhou, L.; Nemeria, N.; Jordan, F.
Amino-terminal residues 1-45 of the Escherichia coli pyruvate dehydrogenase complex E1 subunit interact with the E2 subunit and are required for activity of the complex but not for reductive acetylation of the E2 subunit
Biochemistry
43
14037-14046
2004
Escherichia coli
brenda
Arjunan, P.; Chandrasekhar, K.; Sax, M.; Brunskill, A.; Nemeria, N.; Jordan, F.; Furey, W.
Structural determinants of enzyme binding affinity: the E1 component of pyruvate dehydrogenase from Escherichia coli in complex with the inhibitor thiamin thiazolone diphosphate
Biochemistry
43
2405-2411
2004
Escherichia coli (P0AFG8), Escherichia coli
brenda
Chandrasekhar, K.; Arjunan, P.; Sax, M.; Nemeria, N.; Jordan, F.; Furey, W.
Active-site changes in the pyruvate dehydrogenase multienzyme complex E1 apoenzyme component from Escherichia coli observed at 2.32 A resolution
Acta crystallogr. Sect. D
62
1382-1386
2006
Escherichia coli (P0AFG8), Escherichia coli
brenda
Arjunan, P.; Sax, M.; Brunskill, A.; Chandrasekhar, K.; Nemeria, N.; Zhang, S.; Jordan, F.; Furey, W.
A thiamin-bound, pre-decarboxylation reaction intermediate analogue in the pyruvate dehydrogenase E1 subunit induces large scale disorder-to-order transformations in the enzyme and reveals novel structural features in the covalently bound adduct
J. Biol. Chem.
281
15296-15303
2006
Escherichia coli (P0AFG8), Escherichia coli
brenda
Xiong, Y.; Li, Y.; He, H.; Zhan, C.G.
Theoretical calculation of the binding free energies for pyruvate dehydrogenase E1 binding with ligands
Bioorg. Med. Chem. Lett.
17
5186-5190
2007
Escherichia coli
brenda
Peng, H.; Wang, T.; Xie, P.; Chen, T.; He, H.W.; Wan, J.
Molecular docking and three-dimensional quantitative structure-activity relationship studies on the binding modes of herbicidal 1-(substituted phenoxyacetoxy)alkylphosphonates to the E1 component of pyruvate dehydrogenase
J. Agric. Food Chem.
55
1871-1880
2007
Escherichia coli (P0AFG8)
brenda
Kale, S.; Arjunan, P.; Furey, W.; Jordan, F.
A dynamic loop at the active center of the Escherichia coli pyruvate dehydrogenase complex E1 component modulates substrate utilization and chemical communication with the E2 component
J. Biol. Chem.
282
28106-28116
2007
Escherichia coli (P0AFG8), Escherichia coli
brenda
Kale, S.; Ulas, G.; Song, J.; Brudvig, G.W.; Furey, W.; Jordan, F.
Efficient coupling of catalysis and dynamics in the E1 component of Escherichia coli pyruvate dehydrogenase multienzyme complex
Proc. Natl. Acad. Sci. USA
105
1158-1163
2008
Escherichia coli
brenda
Balakrishnan, A.; Nemeria, N.S.; Chakraborty, S.; Kakalis, L.; Jordan, F.
Determination of pre-steady-state rate constants on the Escherichia coli pyruvate dehydrogenase complex reveals that loop movement controls the rate-limiting step
J. Am. Chem. Soc.
134
18644-18655
2012
Escherichia coli
brenda
Chandrasekhar, K.; Wang, J.; Arjunan, P.; Sax, M.; Park, Y.H.; Nemeria, N.S.; Kumaran, S.; Song, J.; Jordan, F.; Furey, W.
Insight to the interaction of the dihydrolipoamide acetyltransferase (E2) core with the peripheral components in the Escherichia coli pyruvate dehydrogenase complex via multifaceted structural approaches
J. Biol. Chem.
288
15402-15417
2013
Escherichia coli
brenda
He, J.B.; He, H.F.; Zhao, L.L.; Zhang, L.; You, G.Y.; Feng, L.L.; Wan, J.; He, H.W.
Synthesis and antifungal activity of 5-iodo-1,4-disubstituted-1,2,3-triazole derivatives as pyruvate dehydrogenase complex E1 inhibitors
Bioorg. Med. Chem.
23
1395-1401
2015
Escherichia coli
brenda
He, J.; He, H.; Cai, M.; Zhao, F.; He, H.
Insight into the halogen bonding between PA-1 ligand and pyruvate dehydrogenase complex E1 component by crystal structure, DFT calculation, and molecular docking
J. Mol. Struct.
1199
126991
2020
Escherichia coli (P0AFG8)
-
brenda
Yang, M.; Zhang, X.
Construction of pyruvate producing strain with intact pyruvate dehydrogenase and genome-wide transcription analysis
World J. Microbiol. Biotechnol.
33
59
2017
Escherichia coli (P0AFG8), Escherichia coli MG1655 (P0AFG8)
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