Explore the Potential with AI-Driven Innovation
Our detailed focused library is generated on demand with advanced virtual screening and parameter assessment technology powered by the Receptor.AI drug discovery platform. This method surpasses traditional approaches, delivering compounds of better quality with enhanced activity, selectivity, and safety.
We pick out particular compounds from an extensive virtual database of more than 60 billion molecules. The preparation and shipment of these compounds are facilitated by our associate 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 employ our advanced, specialised process to create targeted libraries for enzymes.
Fig. 1. The sreening workflow of Receptor.AI
The procedure entails thorough molecular simulations of the catalytic and allosteric binding pockets, accompanied by ensemble virtual screening that factors in their conformational flexibility. When developing modulators, the structural modifications brought about by reaction intermediates are factored in to optimize activity and selectivity.
Key features that set our library apart include:
partner
Reaxense
upacc
Q8N159
UPID:
NAGS_HUMAN
Alternative names:
Amino-acid acetyltransferase
Alternative UPACC:
Q8N159; B2RAZ9; Q8IWR4
Background:
N-acetylglutamate synthase, mitochondrial, also known as Amino-acid acetyltransferase, plays a crucial role in ureagenesis by synthesizing N-acetylglutamate (NAG). NAG acts as an essential cofactor, modulating the activity of carbamoylphosphate synthase I (CPS1), a key enzyme in the urea cycle.
Therapeutic significance:
N-acetylglutamate synthase deficiency, a rare metabolic disorder, manifests as severe hyperammonemia, developmental delays, and neurological issues. This condition underscores the protein's critical role in metabolic pathways, highlighting the potential for targeted therapeutic strategies to manage or correct the enzyme's activity.