Enzymes
| UniProtKB help_outline | 1,152 proteins |
| Enzyme class help_outline |
|
| GO Molecular Function help_outline |
|
Reaction participants Show >> << Hide
-
Namehelp_outline
O-phospho-L-seryl-[pyruvate dehydrogenase E1 α subunit]
Identifier
RHEA-COMP:13690
Reactive part
help_outline
- Name help_outline O-phospho-L-serine residue Identifier CHEBI:83421 Charge -2 Formula C3H4NO5P SMILEShelp_outline [O-]P([O-])(=O)OC[C@H](N-*)C(-*)=O 2D coordinates Mol file for the small molecule Search links Involved in 25 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,337 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
-
Namehelp_outline
L-seryl-[pyruvate dehydrogenase E1 α subunit]
Identifier
RHEA-COMP:13689
Reactive part
help_outline
- Name help_outline L-serine residue Identifier CHEBI:29999 Charge 0 Formula C3H5NO2 SMILEShelp_outline C([C@H](CO)N*)(=O)* 2D coordinates Mol file for the small molecule Search links Involved in 72 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline phosphate Identifier CHEBI:43474 Charge -2 Formula HO4P InChIKeyhelp_outline NBIIXXVUZAFLBC-UHFFFAOYSA-L SMILEShelp_outline OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1,020 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:12669 | RHEA:12670 | RHEA:12671 | RHEA:12672 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
|||
| EC numbers help_outline | ||||
| Gene Ontology help_outline | ||||
| KEGG help_outline | ||||
| MetaCyc help_outline |
Related reactions help_outline
More general form(s) of this reaction
Publications
-
Yeast pyruvate dehydrogenase complex is regulated by a concerted activity of two kinases and two phosphatases.
Gey U., Czupalla C., Hoflack B., Rodel G., Krause-Buchholz U.
The activity of yeast pyruvate dehydrogenase complex is regulated by reversible phosphorylation. Recently we identified two enzymes that are involved in the phosphorylation (Pkp1p) and dephosphorylation (Ppp1p) of Pda1p, the alpha-subunit of the pyruvate dehydrogenase complex. Here we provide evid ... >> More
The activity of yeast pyruvate dehydrogenase complex is regulated by reversible phosphorylation. Recently we identified two enzymes that are involved in the phosphorylation (Pkp1p) and dephosphorylation (Ppp1p) of Pda1p, the alpha-subunit of the pyruvate dehydrogenase complex. Here we provide evidence that two additional mitochondrial proteins, Pkp2p (Ygl059wp) and Ppp2p (Ycr079wp), are engaged in the regulation of this complex by affecting the phosphorylation state of Pda1p. Our data indicate complementary activities of the kinases and a redundant function for the phosphatases. Both proteins are associated with the complex. We propose a model for the role of the regulatory enzymes and the phosphorylation state of Pda1p in the assembly process of the pyruvate dehydrogenase complex. << Less
-
Regulation of mammalian pyruvate and branched-chain alpha-keto acid dehydrogenase complexes by phosphorylation-dephosphorylation.
Reed L.J., Damuni Z., Merryfield M.L.
-
-Keto acid dehydrogenase complexes. XV. Purification and properties of the component enzymes of the pyruvate dehydrogenase complexes from bovine kidney and heart.
Linn T.C., Pelley J.W., Pettit F.H., Hucho F., Randall D.D., Reed L.J.
Arch Biochem Biophys 148:327-342(1972) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.