EC number:3.1.3.43

Enzyme

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EC Tree
     3. Hydrolases
        3.1 Acting on ester bonds
            3.1.3 Phosphoric-monoester hydrolases
ID:3.1.3.43
Description:[Pyruvate dehydrogenase (acetyl-transferring)]-phosphatase.
Prosite: PDOC00792;
PDB:
PDBScop
Cath: 3.60.40.10;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.1.3.43
BRENDA Enzyme Link: BRENDA 3.1.3.43
KEGG Enzyme Link: KEGG3.1.3.43
BioCyc Enzyme Link: BioCyc 3.1.3.43
ExPASy Enzyme Link: ExPASy3.1.3.43
EC2PDB Enzyme Link: EC2PDB 3.1.3.43
ExplorEnz Enzyme Link: ExplorEnz 3.1.3.43
PRIAM enzyme-specific profiles Link: PRIAM 3.1.3.43
IntEnz Enzyme Link: IntEnz 3.1.3.43
MEDLINE Enzyme Link: MEDLINE 3.1.3.43

EC number:3.1.3.43

MSA:

3.1.3.43;
Phylogenetic Tree:

3.1.3.43;
Uniprot:
M-CSA:
RHEA:12669 [pyruvate dehydrogenase E1 alpha subunit]-O-phospho-L-serine + H2O = [pyruvate dehydrogenase E1 alpha subunit]-L-serine + phosphate
RULE(radius=1) [*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[O;H0;+0:5]-[*:6].[OH2;+0:7]>>[*:6]-[OH;+0:5].[*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[OH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
-Keto acid dehydrogenase complexes. XV. Purification and properties of the component enzymes of the pyruvate dehydrogenase complexes from bovine kidney and heart.Linn TC, Pelley JW, Pettit FH, Hucho F, Randall DD, Reed LJ1972 Feb4401694
Regulation of mammalian pyruvate and branched-chain alpha-keto acid dehydrogenase complexes by phosphorylation-dephosphorylation.Reed LJ, Damuni Z, Merryfield ML19853004826
Yeast pyruvate dehydrogenase complex is regulated by a concerted activity of two kinases and two phosphatases.Gey U, Czupalla C, Hoflack B, Rödel G, Krause-Buchholz U2008 Apr 1118180296