Relation Results

Summary

Name PDH
Primary ID SIGNOR-C402
Links CPX-6233
Type complex
Formed by DLAT, PDHX, DLD, PDHB, PDHA1, PDHA2
Relations 9
Pathways Citric acid cycle, Glycolysis and Gluconeogenesis

Viewer

Type: Score: Layout: SPV 
0.8510.20.9340.80.6560.630.8020.810.851DLDPDHRIPK3PDHBacetyl-CoAPDHA2PDK1PDHA1PDHXDLAT

Relations

Regulator
Mechanism
target
score
+ form complex img/form-complex.png binding PDH 0.851
Identifier Residue Sequence Organism Cell Line
SIGNOR-266545 Homo sapiens
pmid sentence
The human (h) pyruvate dehydrogenase complex (hPDC) 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. Mammalian PDC has a well organized structure with an icosahedral symmetry of the central E2/BP core to which the other component proteins bind non-covalently.
Publications: 1 Organism: Homo Sapiens
Pathways:Citric acid cycle
+ up-regulates activity img/direct-activation.png phosphorylation PDH 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-268065 in vitro
pmid sentence
Here, we show that RIP3 activates the pyruvate dehydrogenase complex (PDC, also known as PDH), the rate-limiting enzyme linking glycolysis to aerobic respiration, by directly phosphorylating the PDC E3 subunit (PDC-E3) on T135.
Publications: 1 Organism: In Vitro
+ form complex img/form-complex.png binding PDH 0.934
Identifier Residue Sequence Organism Cell Line
SIGNOR-266547 Homo sapiens
pmid sentence
The human (h) pyruvate dehydrogenase complex (hPDC) 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. Mammalian PDC has a well organized structure with an icosahedral symmetry of the central E2/BP core to which the other component proteins bind non-covalently.
Publications: 1 Organism: Homo Sapiens
+ up-regulates quantity img/direct-activation.png chemical modification acetyl-CoA 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-266541 Homo sapiens
pmid sentence
The mitochondrial pyruvate dehydrogenase complex (PDC) irreversibly decarboxylates pyruvate to acetyl coenzyme A, thereby linking glycolysis to the tricarboxylic acid cycle and defining a critical step in cellular bioenergetics.
Publications: 1 Organism: Homo Sapiens
Pathways:Citric acid cycle, Glycolysis and Gluconeogenesis
+ form complex img/form-complex.png binding PDH 0.656
Identifier Residue Sequence Organism Cell Line
SIGNOR-267832 Homo sapiens
pmid sentence
The human (h) pyruvate dehydrogenase complex (hPDC) 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. Mammalian PDC has a well organized structure with an icosahedral symmetry of the central E2/BP core to which the other component proteins bind non-covalently.
Publications: 1 Organism: Homo Sapiens
+ down-regulates activity img/direct_inhibition.png phosphorylation PDH 0.63
Identifier Residue Sequence Organism Cell Line
SIGNOR-267445 Homo sapiens P493-6 Cell
pmid sentence
PDK1 is a direct HIF-1 target gene. We found that the gene encoding pyruvate dehydrogenase kinase 1 (PDK1) is a direct target of HIF-1. PDK1 phosphorylates the pyruvate dehydrogenase (PDH) E1α subunit and inactivates the PDH enzyme complex that converts pyruvate to acetyl-coenzyme A, thereby inhibiting pyruvate metabolism via the tricarboxylic acid (TCA) cycle
Publications: 1 Organism: Homo Sapiens
Pathways:Glycolysis and Gluconeogenesis
+ form complex img/form-complex.png binding PDH 0.802
Identifier Residue Sequence Organism Cell Line
SIGNOR-266544 Homo sapiens
pmid sentence
The human (h) pyruvate dehydrogenase complex (hPDC) 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. Mammalian PDC has a well organized structure with an icosahedral symmetry of the central E2/BP core to which the other component proteins bind non-covalently.
Publications: 1 Organism: Homo Sapiens
+ form complex img/form-complex.png binding PDH 0.81
Identifier Residue Sequence Organism Cell Line
SIGNOR-266543 Homo sapiens
pmid sentence
The human (h) pyruvate dehydrogenase complex (hPDC) 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. Mammalian PDC has a well organized structure with an icosahedral symmetry of the central E2/BP core to which the other component proteins bind non-covalently.
Publications: 1 Organism: Homo Sapiens
+ form complex img/form-complex.png binding PDH 0.851
Identifier Residue Sequence Organism Cell Line
SIGNOR-266546 Homo sapiens
pmid sentence
The human (h) pyruvate dehydrogenase complex (hPDC) 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. Mammalian PDC has a well organized structure with an icosahedral symmetry of the central E2/BP core to which the other component proteins bind non-covalently.
Publications: 1 Organism: Homo Sapiens
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