Adenosine Triphosphate: Uridine Monophosphate-Cytidine Monophosphate Phosphotransferase from Tetrahymena pyriformis

Adenosine Triphosphate : Guanosine Monophosphate Phosphotransferase

Several laboratories have reported studies on individual enzymes that belong to the general class of adenosine triphosphate : nucleoside monophosphate phosphotransferases (EC 2.7.4.4), commonly termed nucleoside monophosphate kinases (l-7). Studies with partially purified enzyme preparations have indicated that a variety of nucleoside monophosphates can serve as alternative substrates for nucle...

Adenosine triphosphate: adenosine monophosphate phosphotransferase isozymes in rat liver and hepatomas.

Rat liver adenosine triphosphate: adenosine monophosphate phosphotransferase activity. II. Subcellular localization of adenylate kinase isozymes.

Adenylate kinase activity (ATP:AMP-phosphotransferase, EC 2.7.4.3) was studied in subcellular extracts of rat liver tissue. Essentially all of the activity, over 150 units per g of tissue, wet weight (1.7 units per mg of protein), was released into the cytosol when the tissue was homogenized in 0.025 M sucrose. Isotonic (0.25 M sucrose) homogenization and separation of subcellular fractions by ...

Relationship of adenosine 3',5'-monophosphate to growth and metabolism of Tetrahymena pyriformis.

The concentration of adenosine 3',5'-monophosphate (cyclic AMP) and the activity of adenylate cyclase were determined for the first time in conjuncation with cyclic 3',5'-nucleotide phosphodiesterase (phosphodiesterase) during the growth cycle of Tetrahymena pyriformis. High levels of cyclic AMP observed during early exponential and late stationary phases were associated with elevated adenylate...

Structure of Staphylococcus aureus cytidine monophosphate kinase in complex with cytidine 5′-monophosphate

The crystal structure of Staphylococcus aureus cytidine monophosphate kinase (CMK) in complex with cytidine 5'-monophosphate (CMP) has been determined at 2.3 angstroms resolution. The active site reveals novel features when compared with two orthologues of known structure. Compared with the Streptococcus pneumoniae CMK solution structure of the enzyme alone, S. aureus CMK adopts a more closed c...