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Literature summary for 2.7.1.40 extracted from

  • Pendergrass, D.C.; Williams, R.; Blair, J.B.; Fenton, A.W.
    Mining for allosteric information: natural mutations and positional sequence conservation in pyruvate kinase (2006), IUBMB Life, 58, 31-38.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
A137T increased instability, increased sensitivity to the allosteric inhibitor/product Homo sapiens
G332S mutation alters catalysis and/or protein stability Homo sapiens
G364D mutation alters catalysis and/or protein stability Homo sapiens
G390N mutation alters catalysis and/or protein stability Homo sapiens
R479H mutation does not alter regulation by the activator Homo sapiens
R504L extreme instability Homo sapiens
R510Q increased instability, increased sensitivity to the allosteric inhibitor/product Homo sapiens
R532W loss of allosteric response to the normal activator Homo sapiens
T384M mutation alters catalysis and/or protein stability Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + phosphoenolpyruvate
-
Homo sapiens ATP + pyruvate
-
?

Subunits

Subunits Comment Organism
homotetramer x-ray crystallography Homo sapiens

Synonyms

Synonyms Comment Organism
PYK
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ADP
-
Homo sapiens