|PROSITE documentation PDOC00101
Pyruvate kinase active site signature
Pyruvate kinase (EC 184.108.40.206) (PK)  catalyzes the final step in glycolysis,
the conversion of phosphoenolpyruvate to pyruvate with the concomitant
phosphorylation of ADP to ATP. 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 (gene pykF) and PK-II (gene pykA). All PK isozymes seem to
be tetramers of identical subunits of about 500 amino acid residues.
As a signature pattern for PK we 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.
July 1999 / Pattern and text revised.
PROSITE method (with tools and information) covered by this documentation:
|PYRUVATE_KINASE, PS00110; Pyruvate kinase active site signature (PATTERN)
K is the active site residue; E is a magnesium ligand
|Sequences known to belong to this class detected by the pattern:
|Other sequence(s) detected in Swiss-Prot:
|Matching PDB structures:
1A3W 1A3X 1A49 1A5U ... [ALL]
||Isoenzymes of pyruvate kinase.
||Biochem. Soc. Trans. 18:193-196(1990).
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