| [pyruvate dehydrogenase (lipoamide)] phosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.3.43 | ||||||||
| CAS no. | 9073-70-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
The enzyme [pyruvate dehydrogenase (acetyl-transferring)]-phosphatase (EC 3.1.3.43) catalyzes the reaction
- [pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O [pyruvate dehydrogenase (acetyl-transferring)] + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is [pyruvate dehydrogenase (acetyl-transferring)]-phosphate phosphohydrolase. Other names in common use include pyruvate dehydrogenase phosphatase, phosphopyruvate dehydrogenase phosphatase, [pyruvate dehydrogenase (lipoamide)]-phosphatase, and [pyruvate dehydrogenase (lipoamide)]-phosphate phosphohydrolase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2PNQ.
References
- Linn TC, Pelley JW, Pettit FH, Hucho F, Randall DD, Reed LJ (1972). "α-Keto acid dehydrogenase complexes. XV. Purification and properties of the component enzymes of the pyruvate dehydrogenase complexes from bovine kidney and heart". Arch. Biochem. Biophys. 148 (2): 327–42. doi: 10.1016/0003-9861(72)90151-8. PMID 4401694.
- Reed LJ, Damuni Z, Merryfield ML (1985). "Regulation of mammalian pyruvate and branched-chain α-keto acid dehydrogenase complexes by phosphorylation-dephosphorylation". Curr. Top. Cell. Regul. Current Topics in Cellular Regulation. 27: 41–9. doi: 10.1016/b978-0-12-152827-0.50011-6. ISBN 9780121528270. PMID 3004826.
| [pyruvate dehydrogenase (lipoamide)] phosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.3.43 | ||||||||
| CAS no. | 9073-70-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
The enzyme [pyruvate dehydrogenase (acetyl-transferring)]-phosphatase (EC 3.1.3.43) catalyzes the reaction
- [pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O [pyruvate dehydrogenase (acetyl-transferring)] + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is [pyruvate dehydrogenase (acetyl-transferring)]-phosphate phosphohydrolase. Other names in common use include pyruvate dehydrogenase phosphatase, phosphopyruvate dehydrogenase phosphatase, [pyruvate dehydrogenase (lipoamide)]-phosphatase, and [pyruvate dehydrogenase (lipoamide)]-phosphate phosphohydrolase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2PNQ.
References
- Linn TC, Pelley JW, Pettit FH, Hucho F, Randall DD, Reed LJ (1972). "α-Keto acid dehydrogenase complexes. XV. Purification and properties of the component enzymes of the pyruvate dehydrogenase complexes from bovine kidney and heart". Arch. Biochem. Biophys. 148 (2): 327–42. doi: 10.1016/0003-9861(72)90151-8. PMID 4401694.
- Reed LJ, Damuni Z, Merryfield ML (1985). "Regulation of mammalian pyruvate and branched-chain α-keto acid dehydrogenase complexes by phosphorylation-dephosphorylation". Curr. Top. Cell. Regul. Current Topics in Cellular Regulation. 27: 41–9. doi: 10.1016/b978-0-12-152827-0.50011-6. ISBN 9780121528270. PMID 3004826.