Explore the Potential with AI-Driven Innovation
This comprehensive focused library is produced on demand with state-of-the-art virtual screening and parameter assessment technology driven by Receptor.AI drug discovery platform. This approach outperforms traditional methods and provides higher-quality compounds with superior activity, selectivity and safety.
The compounds are cherry-picked from the vast virtual chemical space of over 60B molecules. The synthesis and delivery of compounds is facilitated by our partner Reaxense.
The library includes a list of the most promising modulators annotated with 38 ADME-Tox and 32 physicochemical and drug-likeness parameters. Also, each compound is presented with its optimal docking poses, affinity scores, and activity scores, providing a comprehensive overview.
We use our state-of-the-art dedicated workflow for designing focused libraries for enzymes.
Fig. 1. The sreening workflow of Receptor.AI
It includes in-depth molecular simulations of both the catalytic and allosteric binding pockets, with ensemble virtual screening focusing on their conformational flexibility. For modulators, the process includes considering the structural shifts due to reaction intermediates to boost activity and selectivity.
Several key aspects differentiate our library:
partner
Reaxense
upacc
O75608
UPID:
LYPA1_HUMAN
Alternative names:
Lysophospholipase 1; Lysophospholipase I; Palmitoyl-protein hydrolase
Alternative UPACC:
O75608; O43202; Q9UQF9
Background:
Acyl-protein thioesterase 1, known alternatively as Lysophospholipase 1, Lysophospholipase I, or Palmitoyl-protein hydrolase, plays a crucial role in cellular processes by hydrolyzing fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. It exhibits depalmitoylating activity towards KCNMA1 and potentially ADRB2, alongside its lysophospholipase activity, breaking down various lysophospholipids and contributing to lysophosphatidic acid production during blood coagulation.
Therapeutic significance:
Understanding the role of Acyl-protein thioesterase 1 could open doors to potential therapeutic strategies.