Which enzyme uses a phosphate from ATP to phosphorylate substrates?

Which enzyme uses a phosphate from ATP to phosphorylate substrates?

• A. Kinase
• B. Phosphatase
• C. Phosphorylase
• D. Ligase

Answer: (A)

Enzymes that transfer a phosphate from ATP to another molecule are kinases. When a phosphate group from ATP is added to a substrate, the substrate becomes phosphorylated, which can change its activity, shape, or interactions in signaling and metabolic pathways. The gamma phosphate of ATP is the one typically moved onto the substrate, with the kinase helping this transfer. Phosphatases do the opposite: they remove phosphate groups, reversing phosphorylation. Phosphorylases use inorganic phosphate (Pi) to add a phosphate to a substrate (such as glycogen) without using ATP as the phosphate donor. Ligases catalyze bond formation between molecules and often use ATP to activate substrates for this condensation, but their main role isn’t phosphorylating a substrate directly with a phosphate from ATP.

Enzymes that transfer a phosphate from ATP to another molecule are kinases. When a phosphate group from ATP is added to a substrate, the substrate becomes phosphorylated, which can change its activity, shape, or interactions in signaling and metabolic pathways. The gamma phosphate of ATP is the one typically moved onto the substrate, with the kinase helping this transfer.

Phosphatases do the opposite: they remove phosphate groups, reversing phosphorylation. Phosphorylases use inorganic phosphate (Pi) to add a phosphate to a substrate (such as glycogen) without using ATP as the phosphate donor. Ligases catalyze bond formation between molecules and often use ATP to activate substrates for this condensation, but their main role isn’t phosphorylating a substrate directly with a phosphate from ATP.