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Pyruvate kinase (EC 2.7.1.40) (PK) [1] 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)

Consensus pattern: [LIVAC]-x-[LIVM](2)-[SAPCV]-K-[LIV]-E-[NKRST]-x-[DEQHS]-[GSTA]-[LIVM] K is the active site residue; E is a magnesium ligand Sequences known to belong to this class detected by the pattern: ALL Other sequence(s) detected in Swiss-Prot: 2

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00110 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00110 • Scan Swiss-Prot/TrEMBL entries against PS00110 • view ligand binding statistics

Matching PDB structures: 1A3W 1A3X 1A49 1A5U ... [ALL]

1	Authors	Muirhead H.
	Title	Isoenzymes of pyruvate kinase.
	Source	Biochem. Soc. Trans. 18:193-196(1990).
	PubMed ID	2379684

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