Enzyme - EC 2.7.1.40 - Pyruvate kinase
|
|||||
Click on the image to start downloading the PDB file (tridimensional and interactive). |
|||||
|
|||||
EC
|
2.7.1.40
|
||||
Official Name
|
pyruvate quinase
|
||||
Alternative Name(s)
|
Phosphoenolpyruvate kinase
Phosphoenol transphosphorylase |
||||
Class
|
2.Transferases 7.Transferring phosphorus-containing groups 1.Phosphotransferases with an alcohol group as acceptor |
||||
Catalysed reaction
|
ATP + pyruvate ADP
+ phosphoenolpyruvate
|
||||
Substrates
|
ATP
UTP GTP CTP ITP dATP pyruvate hydroxylamina Fluorida |
||||
Products
|
ADP
UDP GDP CDP IDP dADP phosphoenolpyruvate O-phosphorilhydroxylamine |
||||
Cofactor(s)
|
CO2
|
||||
Metabolic Pathways
|
|||||
Other comments
|
TP, GTP, CTP, ITP and dATP can also act as donors. Also phosphorylates hydroxylamine and fluoride in the presence of CO2. |
||||
PK requires both magnesium and potassium ions for its activity. PK is found in all living organisms. In vertebrates there are four, tissues specific, isozymes: L (liver), R (red cells), M1 (muscle, heart, and brain), and M2 (early fetal tissues). In Escherichia coli there are two isozymes: PK-I and PK-II. All PK isozymes seem to be tetramers of identical subunits of about 500 amino acid residues. |
|||||
As a signature pattern for PK it has been selected a conserved region that includes a
lysine residue which seems to be the acid/base catalyst responsible for the
interconversion of pyruvate and enolpyruvate, and a glutamic acid residue
implicated in the binding of the magnesium ion. |
|||||
|