Guanylate kinase 2026-11-05
Guanylate kinase is an enzyme that transfers a phosphoryl group from ATP to guanosine monophosphate, producing ADP and guanosine diphosphate:Its official classification is EC 2.7.4.8. The enzyme can also use the corresponding deoxy-nucleotide acceptor and deoxy-ATP donor.[ref]
A constructed mixture containing ATP and guanosine monophosphate, initially without products, permits at most of each product through the forward reaction. At least ATP remains if no other reactions consume it. Per turnover, the phosphate inventory is conserved: .
This ceiling concerns stoichiometry. Reversible chemical equilibrium, substrate concentrations and assay conditions determine the actual conversion; the inventory alone does not specify an enzyme rate.
In 1992, M. Konrad isolated and characterized the yeast GUK1 gene encoding guanylate kinase, connecting a chemically defined activity with a molecularly identifiable catalyst.[ref]
Cloning and expression of the essential gene for guanylate kinase from yeast by M. Konrad. Abstract, reversible phosphoryl transfer and gene identification
The kinase reaction should also be distinguished from guanylate cyclase, which converts GTP to a cyclic nucleotide rather than transferring ATP's terminal phosphoryl group to GMP. M. Konrad 2026-11-05
M. Konrad authored a 1992 study isolating and characterizing the Saccharomyces cerevisiae gene for guanylate kinase. The enzyme transfers a terminal phosphoryl group from ATP to guanosine monophosphate, producing ADP and guanosine diphosphate in a reversible reaction.[ref]
Cloning and expression of the essential gene for guanylate kinase from yeast by M. Konrad. Abstract: reaction and gene isolation
Disrupting the gene caused recessive lethality, supporting its necessity for vegetative growth under the tested conditions. Inducible gene expression also produced large quantities of guanylate kinase in both Saccharomyces cerevisiae and Escherichia coli.[ref]
Cloning and expression of the essential gene for guanylate kinase from yeast by M. Konrad. Abstract: insertional mutation and expression systems
These interventions addressed complementary questions. Loss of function tested whether the native system could grow without the gene's contribution; increased expression made the protein available for biochemical measurements. The ability to express a protein abundantly does not by itself establish that the corresponding gene is essential.