Pyruvate Kinase

Pyruvate kinase is the enzyme in glycolysis that catalyzes the final step of glycolysis.  In this reaction, a phosphoryl group is transferred from phosphoenolpyruvate to ADP (Figure 1).  In this virtually irreversible reaction, pyruvate is formed, and one ATP is generated.

 ^-O OPO₃^2-     ADP+H⁺     ATP            O^-
  | |             \_____/               |
O=C-C=C-H     ------------------>   O=C-C=O
      |         pyruvate kinase         |
      H                                 CH₃
phosphoenolpyruvate                              pyruvate
 

Figure 1.  The catalytic action of pyruvate kinase.  (Stryer 1995)

The structure of pyruvate kinase (Oryctolagus cuniculus pyruvate kinase mRNA, partial cds.) can be seen by clicking on the following link:  RasMol image of pyruvate kinase.  (MMDB Id: 1915,  PDB Id: 1PKN)

Of interest to many scientists is the amino acid sequence and corresponding base pair sequence of the protein.  Pyruvate kinase has been sequenced for a number of organisms.  Five such sequences are given below.  Click on the name of the organism to see its sequences.

Saccharomyces cerevisiae
Oryctolagus cuniculus
Mus musculus
Homo sapiens
Chlamydia trachomatis

Stryer, L.  Biochemistry, 4th ed.  Stanford University: W. H. Freeman and Company, New York, 1995.
p. 489.

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