Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.11.2 extracted from

  • Kato, M.; Chuang, J.L.; Tso, S.C.; Wynn, R.M.; Chuang, D.T.
    Crystal structure of pyruvate dehydrogenase kinase 3 bound to lipoyl domain 2 of human pyruvate dehydrogenase complex (2005), EMBO J., 24, 1763-1774.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.11.2

Activating Compound

Activating Compound Comment Organism Structure
L2 domain of pyruvate dehydrogenase complex binding to the inner lipoyl domains L2 of E2 component activate the enzyme by conformational changes and disrupting the ATP lid and eliminating product inhibition by ADP, binding structure, overview, L2 binding increases affinities for both ADP and ATP Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
pyruvate dehydrogenase kinase 3 bound to ATP and the lipoyl domain 2 of human pyruvate dehydrogenase complex, X-ray structure determination and analysis at 1.0 A resolution, modeling of closed and open conformation Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
ADP product inhibition, L2 binding increases affinities for both ADP and ATP Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information dissociation constants for ADP and ATP binding, L2 binding increases affinities for both ADP and ATP Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + pyruvate dehydrogenase Homo sapiens
-
 ADP + phosphorylated pyruvate dehydrogenase
-
 ir

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + [pyruvate dehydrogenase (acetyl-transferring)] = ADP + [pyruvate dehydrogenase (acetyl-transferring)]phosphate allosteric R-T equilibrium as the mechanism for L2-stimulated PDK3 activity, the active cleft undergoes a conformational change from closed to open conformation upon stimulation by L2 binding releasing ADP Homo sapiens
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + pyruvate dehydrogenase
-
 Homo sapiens ADP + phosphorylated pyruvate dehydrogenase
-
 ir
ATP + pyruvate dehydrogenase phosphorylation of serine residues of the E1 component of pyruvate dehydrogenase complex PDC Homo sapiens ADP + phosphorylated pyruvate dehydrogenase
-
 ir

Subunits

Subunits Comment Organism
dimer PDK is a component of the pyruvate dehydrogenase complex bound to the inner lipoyl domains, i.e. L2, of the E2 component, the C-terminus of one PDK subunit constitutes an integral part of the lipoyl-binding pocket in the N-terminus of the opposing other subunit Homo sapiens

Synonyms

Synonyms Comment Organism
PDK3
-
 Homo sapiens
pyruvate dehydrogenase kinase 3
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP L2 binding increases affinities for both ADP and ATP Homo sapiens
ATPgammaS dissociation constants as ATP in binding to PDK3 Homo sapiens