Guanylate kinase

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 $3\mu \mathrm{mol}$ ATP and $2\mu \mathrm{mol}$ guanosine monophosphate, initially without products, permits at most $2\mu \mathrm{mol}$ of each product through the forward reaction. At least $1\mu \mathrm{mol}$ ATP remains if no other reactions consume it. Per turnover, the phosphate inventory is conserved: $3+1=2+2$.

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] 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.