+ |
PDK3 | down-regulates activity
phosphorylation
|
PDHA1 |
0.866 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-109613 |
Ser232 |
NRYGMGTsVERAAAS |
in vitro |
|
pmid |
sentence |
11485553 |
Here we report that the four isoenzymes of protein kinase responsible for the phosphorylation and inactivation of pyruvate dehydrogenase (pdk1, pdk2, pdk3 and pdk4) differ in their abilities to phosphorylate the enzyme. Pdk1 can phosphorylate all three sites (s232, s293, s300), whereas pdk2, pdk3 and pdk4 each phosphorylate only s232 and s293. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-109609 |
Ser293 |
TYRYHGHsMSDPGVS |
in vitro |
|
pmid |
sentence |
11485553 |
Here we report that the four isoenzymes of protein kinase responsible for the phosphorylation and inactivation of pyruvate dehydrogenase (pdk1, pdk2, pdk3 and pdk4) differ in their abilities to phosphorylate the enzyme. Pdk1 can phosphorylate all three sites (s232, s293, s300), whereas pdk2, pdk3 and pdk4 each phosphorylate only s232 and s293. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-109647 |
Ser293 |
TYRYHGHsMSDPGVS |
in vitro |
|
pmid |
sentence |
11486000 |
Activity of the mammalian pyruvate dehydrogenase complex is regulated by phosphorylation-dephosphorylation of the alpha subunit of the pyruvate dehydrogenase (e1) component. Phosphorylation is carried out by four pyruvate dehydrogenase kinase (pdk) isoenzymes. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-109651 |
Ser300 |
SMSDPGVsYRTREEI |
in vitro |
|
pmid |
sentence |
11486000 |
Activity of the mammalian pyruvate dehydrogenase complex is regulated by phosphorylation-dephosphorylation of the alpha subunit of the pyruvate dehydrogenase (e1) component. Phosphorylation is carried out by four pyruvate dehydrogenase kinase (pdk) isoenzymes. |
|
Publications: |
4 |
Organism: |
In Vitro |
+ |
PDK3 | down-regulates
phosphorylation
|
PDHA2 |
0.544 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-143974 |
Ser291 |
TYRYHGHsMSDPGVS |
Homo sapiens |
|
pmid |
sentence |
16436377 |
Pdh2 was found to be very similar to pdh1 / in the mechanism of inactivation by phosphorylation of three sites;and (iv) in the phosphorylation of sites 1 and 2 by pdk3 / (ser-264 (site 1), ser-271 (site 2), and ser-203 (site 3) |
|
Publications: |
1 |
Organism: |
Homo Sapiens |