| + |
PDHA2 | form complex 
binding
|
PDH |
0.656 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267832 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20160912 |
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 |
| + |
DLD | form complex
binding
|
PDH |
0.851 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266545 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20160912 |
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 |
| + |
PDK1 | down-regulates activity 
phosphorylation
|
PDH |
0.629 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267445 |
|
|
Homo sapiens |
P493-6 Cell |
| pmid |
sentence |
| 16517405 |
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 |
| + |
PDHA1 | form complex
binding
|
PDH |
0.801 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266544 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20160912 |
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 |
| + |
RIPK3 | up-regulates activity 
phosphorylation
|
PDH |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268065 |
|
|
in vitro |
|
| pmid |
sentence |
| 29358703 |
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 |
| + |
PDH | up-regulates quantity
chemical modification
|
acetyl-CoA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266541 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29059435 |
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 |
| + |
PDHB | form complex
binding
|
PDH |
0.934 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266547 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20160912 |
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 |
| + |
DLAT | form complex
binding
|
PDH |
0.85 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266546 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20160912 |
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 |
| + |
PDHX | form complex
binding
|
PDH |
0.809 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266543 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20160912 |
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 |
3.0
PDH
CPX-6233