Pyruvate dehydrogenase
| pyruvate dehydrogenase (acetyl-transferring) | |||||||||
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Crystallographic structure of pyruvate dehydrogenase (PDH). PH is a six domain dimer with α (blue), α’ (yellow), β (red), and β’ (teal) regions denoted by the different colors. Thiamine pyrophosphate (TPP) is shown in grey ball and stick form, two magnesium ions in purple undergoing metal ligation with the TPP, and two potassium ions in orange.
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| Identifiers | |||||||||
| EC number | 1.2.4.1 | ||||||||
| CAS number | 9014-20-4 | ||||||||
| 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 / EGO | ||||||||
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| Search | |
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| PMC | articles |
| PubMed | articles |
| NCBI | proteins |
| Pyruvate dehydrogenase (lipoamide) alpha 1 | |
|---|---|
| Identifiers | |
| Symbol | PDHA1 |
| Alt. symbols | PDHA |
| Entrez | 5160 |
| HUGO | 8806 |
| OMIM | 300502 |
| RefSeq | NM_000284 |
| UniProt | P08559 |
| Other data | |
| EC number | 1.2.4.1 |
| Locus | Chr. X p22.1 |
| pyruvate dehydrogenase (lipoamide) alpha 2 | |
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| Identifiers | |
| Symbol | PDHA2 |
| Alt. symbols | PDHAL |
| Entrez | 5161 |
| HUGO | 8807 |
| OMIM | 179061 |
| RefSeq | NM_005390 |
| UniProt | P29803 |
| Other data | |
| EC number | 1.2.4.1 |
| Locus | Chr. 4 q22-q23 |
| pyruvate dehydrogenase (lipoamide) beta | |
|---|---|
| Identifiers | |
| Symbol | PDHB |
| Alt. symbols | PHE1B |
| Entrez | 5162 |
| HUGO | 8808 |
| OMIM | 179060 |
| RefSeq | NM_000925 |
| UniProt | P11177 |
| Other data | |
| EC number | 1.2.4.1 |
| Locus | Chr. 3 p21.1-14.2 |
Pyruvate dehydrogenase is the first component enzyme of pyruvate dehydrogenase complex (PDC). The pyruvate dehydrogenase complex contributes to transforming pyruvate into acetyl-CoA by a process called pyruvate decarboxylation (Swanson Conversion). Acetyl-CoA may then be used in the citric acid cycle to carry out cellular respiration, so pyruvate dehydrogenase contributes to linking the glycolysis metabolic pathway to the citric acid cycle and releasing energy via NADH.
Pyruvate dehydrogenase (E1) performs the first two reactions within the pyruvate dehydrogenase complex (PDC): a decarboxylation of substrate 1 (pyruvate) and a reductive acetylation of substrate 2 (lipoic acid). Lipoic acid is covalently bound to dihydrolipoamide acetyltransferase (E2), which is the second catalytic component enzyme of PDC. The reaction catalyzed by pyruvate dehydrogenase (E1) is considered to be the rate-limiting step for the pyruvate dehydrogenase complex (PDHc).
Phosphorylation of E1 by pyruvate dehydrogenase kinase (PDK) inactivates E1 and subsequently the entire complex. PDK is inhibited by dichloroacetic acid and pyruvate, resulting in a higher quantity of active, unphosphorylated PDH. Phosphorylaton is reversed by pyruvate dehydrogenase phosphatase, which is stimulated by insulin, PEP, and AMP, but competitively inhibited by ATP, NADH, and Acetyl-CoA.
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