ATPst

ATPst, short for ATP stabilizer, is a fictional biochemical molecule used in educational and speculative contexts to explore ATP-dependent processes. It is not an actual compound recognized by current biochemical literature.

In these contexts, ATPst is described as a non-hydrolyzable ligand that binds to ATP-binding pockets of enzymes with high affinity while resisting cleavage of the terminal phosphate. Its hypothetical structure is imagined to feature a modified gamma-phosphate or a chemically inert substituent that maintains pocket recognition but prevents energy transfer.

Applications in fiction and pedagogy include illustrating how enzymes undergo conformational changes upon nucleotide binding, separating binding from catalysis, and modeling energy flow in pathways. ATPst can be used in thought experiments, simulations, and classroom demonstrations to discuss the difference between substrate binding and catalytic turnover.

Real-world analogs exist; non-hydrolyzable ATP analogs such as AMP-PNP and ATPγS are used in actual biochemistry for similar purposes, though they are distinct compounds. Because ATPst is fictional, it should not be conflated with real molecules, and references to it are confined to explanatory or narrative contexts.