+ |
RIPK3 | up-regulates activity
phosphorylation
|
DLD |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266372 |
Thr135 |
STAVKALtGGIAHLF |
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 |
+ |
DLD | form complex
binding
|
Glycine cleavage system |
0.634 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268243 |
|
|
Homo sapiens |
|
pmid |
sentence |
16051266 |
The glycine cleavage system is a mitochondrial multienzyme system composed of four proteins termed P, H, T and L-protein, and catalyzes the reversible oxidation of glycine yielding carbon dioxide, ammonia, 5,10-methylenetetrahydrofolate (5,10-CH2-H4folate), and reduced pyridine nucleotide. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
DLD | form complex
binding
|
OGDC |
0.849 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266256 |
|
|
Homo sapiens |
|
pmid |
sentence |
15953811 |
The α-ketoglutarate–dehydrogenase complex is a complex including multiple copies of three proteins: E1k (α-ketoglutarate dehydrogenase), E2k (dihydrolipoyl succinyltransferase), and E3 (dihydrolipoamide dehydrogenase) (Fig. 2). The consecutive action of the three catalytic components of KGDHC results in oxidative decarboxylation of 2-oxoglutarate, preserving the energy in the form of succinylCoA and NADH. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Citric acid cycle |
+ |
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 |