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Information on EC 1.2.4.1 - pyruvate dehydrogenase (acetyl-transferring) and Organism(s) Homo sapiens and UniProt Accession P08559

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IUBMB Comments
Contains thiamine diphosphate. It is a component (in multiple copies) of the multienzyme pyruvate dehydrogenase complex in which it is bound to a core of molecules of EC 2.3.1.12, dihydrolipoyllysine-residue acetyltransferase, which also binds multiple copies of EC 1.8.1.4, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.12.
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This record set is specific for:
Homo sapiens
UNIPROT: P08559
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The taxonomic range for the selected organisms is: Homo sapiens
Synonyms
pdh, pdh complex, e1alpha, mitochondrial pyruvate dehydrogenase, pyruvate dehydrogenase multienzyme complex, pdhc-e1, pyruvate dehydrogenase e1, mtpdc, pdhc e1, pdh e1alpha, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydrogenase, pyruvate
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-
-
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E1p
247
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mitochondrial pyruvate dehydrogenase
247
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MtPDC
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-
-
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PDH complex
247
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PDH-E1 catalytic subunit
247
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PDHalpha
247
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PDHC
247
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PDHc-E1
284096
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PDHE1alpha
284096
E1 alpha subunit of pyruvate dehydrogenase
pyruvate decarboxylase
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-
-
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pyruvate dehydrogenase
-
-
-
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pyruvate dehydrogenase alpha subunit
247
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pyruvate dehydrogenase complex
pyruvate dehydrogenase E1
pyruvate dehydrogenase E1 alpha subunit
247
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pyruvate dehydrogenase multienzyme complex
284096
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pyruvic acid dehydrogenase
-
-
-
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pyruvic dehydrogenase
-
-
-
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thiamin-dependent pyruvate dehydrogenase
284096
part of the pyruvate dehydrogenase multienzyme complex PDHc as component E1
VEG220
-
-
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Vegetative protein 220
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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-
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reduction
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SYSTEMATIC NAME
IUBMB Comments
pyruvate:[dihydrolipoyllysine-residue acetyltransferase]-lipoyllysine 2-oxidoreductase (decarboxylating, acceptor-acetylating)
Contains thiamine diphosphate. It is a component (in multiple copies) of the multienzyme pyruvate dehydrogenase complex in which it is bound to a core of molecules of EC 2.3.1.12, dihydrolipoyllysine-residue acetyltransferase, which also binds multiple copies of EC 1.8.1.4, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.12.
CAS REGISTRY NUMBER
COMMENTARY hide
9014-20-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
show the reaction diagram
2-hydroxyethylidene-thiamine diphosphate + 2,6-dichlorophenolindophenol
S-acetyldihydrolipoamide + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
acetaldehyde + benzaldehyde
(R)-phenylacetylcarbinol
show the reaction diagram
-
-
-
-
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pyruvate + acetylphosphinate + NAD+
(R)-acetoin + ? + NADH
show the reaction diagram
-
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
show the reaction diagram
pyruvate + CoA + oxidized 2,6-dichlorophenolindophenol
acetyl-CoA + CO2 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
show the reaction diagram
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
show the reaction diagram
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-
-
ir
additional information
?
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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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
thiamine diphosphate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetylmethylphosphinate
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partially reversible tight-binding inhibitor, formation of a C2alpha-phosphinolactylthiamine diphosphate derivative involving H63 residue of enzyme
Acetylphosphinate
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partially reversible tight-binding inhibitor, formation of a C2alpha-phosphinolactylthiamine diphosphate derivative involving H63 residue of enzyme
methyl acetylphosphonate
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phosphonate analogue of pyruvate, leading to formation of a stable 1’,4’-imino-2-alpha-phosphonolactyl-thiamindiphosphate
Phosphorylation
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phosphorylation inactivates recombinant alpha2,beta2 tetramer in about 10 min
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pyruvate dehydrogenase kinase
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phosphorylation of E1p by pyruvate dehydrogenase kinase isoforms inactivates the pyruvate dehydrogenase complex
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thiamine 2-thiothiazolone diphosphate
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-
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AMP
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ascites tumour cells, 1 mM, about 2fold activation of pyruvate dehydrogenase
cAMP
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ascites tumour cells
fatty acid transport protein 1
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enhances mitochondrial pyruvate dehydrogenase activity
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GMP
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ascites tumour cells
pyruvate dehydrogenase kinase
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dephosphorylation by pyruvatedehydrogenase phosphatase isoforms restores pyruvate dehydrogenase complex activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 0.0648
pyruvate
0.0015
thiamine diphosphate
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recombinant enzyme
additional information
additional information
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detailed kinetic and thermodynamic analysis
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.077 - 69.9
pyruvate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00146
acetylmethylphosphinate
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pH 8.0, 30°C
0.000014
Acetylphosphinate
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pH 8.0, 30°C
0.0000737
thiamine 2-thiothiazolone diphosphate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0162
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recombinant His-tagged-alpha2,beta2 tetramer, assay with 2-hydroxyethylidene-thiamine diphosphate and 2,6-dichlorphenolindophenol
0.0269
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recombinant His-tagged-alpha2,beta2 tetramer, assay with pyruvate and 2,6-dichlorphenolindophenol
0.13
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recombinant alpha2beta2 tetramer
0.145
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recombinant alpha2,His-tagged-beta2 tetramer, K3Fe(CN)6 as artificial electron acceptor
0.18
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recombinant alpha2,beta2 tetramer with six histidine residues attached to the N-terminus
0.187
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recombinant His-tagged-alpha2,beta2 tetramer, K3Fe(CN)6 as artificial electron acceptor
0.367
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recombinant alpha2,His-tagged-beta2 tetramer, assay with pyruvate and 2,6-dichlorphenolindophenol
8.13
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recombinant enzyme from liver
10.9
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recombinant alpha2,His-tagged-beta2 tetramer, reduction of NAD+, overall reaction
14.4
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recombinant His-tagged-alpha2,beta2 tetramer, reduction of NAD+, overall reaction
24.6
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pH 7.0, 37°C, isoform PDH2
25.9
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pH 7.0, 37°C, isoform PDH1
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
ODPA_HUMAN
390
0
43296
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
160000
-
recombinant alpha2,beta2 tetramer
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
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the PDC is tightly regulated by reversible phosphorylation at three known phosphorylation sites on PDHE1a: Ser293, Ser300, and Ser232
phosphorylation
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phosphorylation of Ser264 slows the preceding binding of substrate to the enzyme's active site via the substrate channel and the subsequent reductive acetylation of the E2 component
phosphoprotein
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regulation of activity by pyruvate dehydrogenase kinase isoenzymes. PDK2 has the highest activity for site S264 of PDH2, PDK3 has higher activity for site S271 than for site S264, and only PDK1 can phosphorylate site S203
proteolytic modification
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cleavage of 29 amino acid long leader peptide from alpha subunit suggested from deduced protein sequence
side-chain modification
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phosphorylation of recombinant alpha2,beta2 tetramer, 3.25 phosphoryl groups per mol tetramer are incorporated, 50% phosphorylation within 10 min, only the alpha subunit is phosphorylated
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
vapour diffusion method with 14-18% PEG 3350, 0.1 mM sodium azide, and 200 mM NaSCN in 50 mM potassium phosphate (pH 8.0)
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recombinant enzyme, orthorhombic crystals in polyethylene glycol 3350 by vapor-diffusion method, space group P222
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S264E
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pseudophosphorylation mutant, the preceding binding of substrate to the enzyme's active site via the substrate channel and the subsequent reductive acetylation of the E2 component are severely slowed in the mutant enzyme
S264Q
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selectively deficient in pyruvate binding and reductive acetylation of component E2
D289A
D289N
E229A
E229Q
E232A
E232Q
E234A
E234Q
H63A
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about 17% residual activity in assay using 2,6-dichlorophenolindophenol, only modest inhibition by acetylphosphinate and acetylmethylphosphinate
I329A
I329del
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the mutant shows reductions in activities in both the 2,6-dichlorophenolindophenol and PDC assays
M153V
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the mutant shows decreased PDH activity in fibroblasts, around 30% of mean control
Q206L
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the mutant shows decreased PDH activity in fibroblasts, around 52% of mean control
R253G
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the mutation is associated with low PDHc activity and absence of subunit alpha of pyruvate dehydrogenase E1
S203A
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isoform PDH2, mutation of phosphorylation site
S203A/S271A
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phosphorylation at remaining site S264 causes 96% inactivation
S203A/S64A
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phosphorylation at remaining site S271 causes complete inactivation
S203E
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isoform PDH2, mutation of phosphorylation site
S264A
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isoform PDH2, mutation of phosphorylation site, no enzymic activity
S264E
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isoform PDH2, mutation of phosphorylation site
S271A
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isoform PDH2, mutation of phosphorylation site, no enzymic activity
S271E
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isoform PDH2, mutation of phosphorylation site
S64A/S271A
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phosphorylation at remaining site S203 causes 91% inactivation
additional information
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
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recombinant alpha and beta subunits and recombinant alpha2,beta2 tetramer
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli M15 cells
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alpha-subunit
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beta-subunit
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co-expression of alpha subunit with human liver beta subunit in Escherichia coli; expression of alpha and beta subunits in Escherichia coli
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expressed in Escherichia coli BL21 cells
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His-tagged alpha and beta subunits and alpha2,beta2 tetramer, expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ho, L.; Patel, M.S.
Cloning and cDNA sequence of the beta-subunit component of human pyruvate dehydrogenase complex
Gene
86
297-302
1990
Homo sapiens
Manually annotated by BRENDA team
Koike, K.; Urata, Y.; Koike, M.
Molecular cloning and characterization of human pyruvate dehydrogenase beta subunit gene
Proc. Natl. Acad. Sci. USA
87
5594-5597
1990
Homo sapiens
Manually annotated by BRENDA team
Ho, L.; Wexler, I.D.; Liu, T.C.; Thekkumara, T.J.; Patel, M.S.
Characterization of cDNAs encoding human pyruvate dehydrogenase alpha subunit
Proc. Natl. Acad. Sci. USA
86
5330-5334
1989
Homo sapiens
Manually annotated by BRENDA team
Dahl, H.H.M.; Hunt, S.M.; Hutchison, W.M.; Brown, G.K.
The human pyruvate dehydrogenase complex. Isolation of cDNA clones for the E1 alpha subunit, sequence analysis, and characterization of the mRNA
J. Biol. Chem.
262
7398-7403
1987
Homo sapiens
Manually annotated by BRENDA team
Lazo, P.A.; Sols, A.
Pyruvate dehydrogenase complex of ascites tumour. Activation by AMP and other properties of potential significance in metabolic regulation
Biochem. J.
190
705-710
1980
Bos taurus, Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Korotchkina, L.G.; Tucker, M.M.; Thekkumkara, T.J.; Madhusudhan, K.T.; Pons, G.; Kim, H.; Patel, M.S.
Overexpression and characterization of human tetrameric pyruvate dehydrogenase and its individual subunits
Protein Expr. Purif.
6
79-90
1995
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Jeng, J.; Kallarakal, A.T.; Kim, S.F.; Popov, K.M.; Song, B.J.
Pyruvate dehydrogenase E1alpha isoform in rat testis: cDNA cloning, characterization, and biochemical comparison of the recombinant testis and liver enzymes
Comp. Biochem. Physiol. B
120
205-216
1998
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Ciszak, E.; Korotchkina, L.G.; Hong, Y.S.; Joachimiak, A.; Patel, M.S.
Crystallization and initial x-ray diffraction analysis of human pyruvate dehydrogenase
Acta Crystallogr. Sect. D
57
465-468
2001
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Koukourakis, M.I.; Giatromanolaki, A.; Sivridis, E.; Gatter, K.C.; Harris, A.L.
Pyruvate dehydrogenase and pyruvate dehydrogenase kinase expression in non small cell lung cancer and tumor-associated stroma
Neoplasia
7
1-6
2005
Homo sapiens
Manually annotated by BRENDA team
Seifert, F.; Golbik, R.; Brauer, J.; Lilie, H.; Schroeder-Tittmann, K.; Hinze, E.; Korotchkina, L.G.; Patel, M.S.; Tittmann, K.
Direct kinetic evidence for half-of-the-sites reactivity in the E1 component of the human pyruvate dehydrogenase multienzyme complex through alternating sites cofactor activation
Biochemistry
45
12775-12785
2006
Homo sapiens
Manually annotated by BRENDA team
Nemeria, N.S.; Korotchkina, L.G.; Chakraborty, S.; Patel, M.S.; Jordan, F.
Acetylphosphinate is the most potent mechanism-based substrate-like inhibitor of both the human and Escherichia coli pyruvate dehydrogenase components of the pyruvate dehydrogenase complex
Bioorg. Chem.
34
362-379
2006
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Smolle, M.; Prior, A.E.; Brown, A.E.; Cooper, A.; Byron, O.; Lindsay, J.G.
A new level of architectural complexity in the human pyruvate dehydrogenase complex
J. Biol. Chem.
281
19772-19780
2006
Homo sapiens
Manually annotated by BRENDA team
Korotchkina, L.G.; Sidhu, S.; Patel, M.S.
Characterization of testis-specific isoenzyme of human pyruvate dehydrogenase
J. Biol. Chem.
281
9688-9696
2006
Homo sapiens
Manually annotated by BRENDA team
Gurd, B.J.; Peters, S.J.; Heigenhauser, G.J.; LeBlanc, P.J.; Doherty, T.J.; Paterson, D.H.; Kowalchuk, J.M.
O2 uptake kinetics, pyruvate dehydrogenase activity, and muscle deoxygenation in young and older adults during the transition to moderate-intensity exercise
Am. J. Physiol. Regul. Integr. Comp. Physiol.
294
R577-R584
2008
Homo sapiens
Manually annotated by BRENDA team
Seifert, F.; Ciszak, E.; Korotchkina, L.; Golbik, R.; Spinka, M.; Dominiak, P.; Sidhu, S.; Brauer, J.; Patel, M.S.; Tittmann, K.
Phosphorylation of serine 264 impedes active site accessibility in the E1 component of the human pyruvate dehydrogenase multienzyme complex
Biochemistry
46
6277-6287
2007
Homo sapiens, Homo sapiens (P08559)
Manually annotated by BRENDA team
Korotchkina, L.G.; Patel, M.S.
Binding of pyruvate dehydrogenase to the core of the human pyruvate dehydrogenase complex
FEBS Lett.
582
468-472
2008
Homo sapiens
Manually annotated by BRENDA team
Bradley, N.S.; Heigenhauser, G.J.; Roy, B.D.; Staples, E.M.; Inglis, J.G.; LeBlanc, P.J.; Peters, S.J.
The acute effects of differential dietary fatty acids on human skeletal muscle pyruvate dehydrogenase activity
J. Appl. Physiol.
104
1-9
2008
Homo sapiens
Manually annotated by BRENDA team
McFate, T.; Mohyeldin, A.; Lu, H.; Thakar, J.; Henriques, J.; Halim, N.D.; Wu, H.; Schell, M.J.; Tsang, T.M.; Teahan, O.; Zhou, S.; Califano, J.A.; Jeoung, N.H.; Harris, R.A.; Verma, A.
Pyruvate dehydrogenase complex activity controls metabolic and malignant phenotype in cancer cells
J. Biol. Chem.
283
22700-22708
2008
Homo sapiens
Manually annotated by BRENDA team
Yu, X.; Hiromasa, Y.; Tsen, H.; Stoops, J.K.; Roche, T.E.; Zhou, Z.H.
Structures of the human pyruvate dehydrogenase complex cores: a highly conserved catalytic center with flexible N-terminal domains
Structure
16
104-114
2008
Homo sapiens
Manually annotated by BRENDA team
Joao Silva, M.; Pinheiro, A.; Eusebio, F.; Gaspar, A.; Tavares de Almeida, I.; Rivera, I.
Pyruvate dehydrogenase deficiency: identification of a novel mutation in the PDHA1 gene which responds to amino acid supplementation
Eur. J. Pediatr.
168
17-22
2009
Homo sapiens
Manually annotated by BRENDA team
Li, J.; Kato, M.; Chuang, D.T.
Pivotal role of the C-terminal DW-motif in mediating inhibition of pyruvate dehydrogenase kinase 2 by dichloroacetate
J. Biol. Chem.
284
34458-34467
2009
Homo sapiens
Manually annotated by BRENDA team
Ostergaard, E.; Moller, L.B.; Kalkanoglu-Sivri, H.S.; Dursun, A.; Kibaek, M.; Thelle, T.; Christensen, E.; Duno, M.; Wibrand, F.
Four novel PDHA1 mutations in pyruvate dehydrogenase deficiency
J. Inherit. Metab. Dis.
32
S235-S239
2009
Homo sapiens
Manually annotated by BRENDA team
Guitart, M.; Andreu, A.L.; Garcia-Arumi, E.; Briones, P.; Quintana, E.; Gomez-Foix, A.M.; Garcia-Martinez, C.
FATP1 localizes to mitochondria and enhances pyruvate dehydrogenase activity in skeletal myotubes
Mitochondrion
9
266-272
2009
Homo sapiens
Manually annotated by BRENDA team
Glushakova, L.G.; Lisankie, M.J.; Eruslanov, E.B.; Ojano-Dirain, C.; Zolotukhin, I.; Liu, C.; Srivastava, A.; Stacpoole, P.W.
AAV3-mediated transfer and expression of the pyruvate dehydrogenase E1 alpha subunit gene causes metabolic remodeling and apoptosis of human liver cancer cells
Mol. Genet. Metab.
98
289-299
2009
Homo sapiens
Manually annotated by BRENDA team
Rardin, M.J.; Wiley, S.E.; Naviaux, R.K.; Murphy, A.N.; Dixon, J.E.
Monitoring phosphorylation of the pyruvate dehydrogenase complex
Anal. Biochem.
389
157-164
2009
Homo sapiens (P08559), Mus musculus
Manually annotated by BRENDA team
Patel, M.S.; Korotchkina, L.G.; Sidhu, S.
Interaction of E1 and E3 components with the core proteins of the human pyruvate dehydrogenase complex
J. Mol. Catal. B
61
2-6
2009
Homo sapiens
Manually annotated by BRENDA team
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