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.
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.
In the library, a selection of top modulators is provided, each marked with 38 ADME-Tox and 32 parameters related to physicochemical properties and drug-likeness. Also, every compound comes with its best docking poses, affinity scores, and activity scores, providing a comprehensive overview.
Our top-notch dedicated system is used to design specialised libraries for enzymes.
Fig. 1. The sreening workflow of Receptor.AI
It includes comprehensive molecular simulations of the catalytic and allosteric binding pockets and the ensemble virtual screening accounting for their conformational mobility. In the case of designing modulators, the structural changes induced by reaction intermediates are taken into account to leverage activity and selectivity.
Our library stands out due to several important features:
partner
Reaxense
upacc
Q13126
UPID:
MTAP_HUMAN
Alternative names:
5'-methylthioadenosine phosphorylase
Alternative UPACC:
Q13126; I2G7M5; I2G7M6; I2G7M7; I2G7M8; I2G7M9; I2G7N0; Q5T3P3; Q9H010
Background:
S-methyl-5'-thioadenosine phosphorylase, also known as 5'-methylthioadenosine phosphorylase, plays a pivotal role in the methionine salvage pathway. It catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate, crucial for the breakdown of MTA, a by-product of polyamine biosynthesis. This enzyme exhibits broad substrate specificity, with a preference for 6-aminopurine nucleosides.
Therapeutic significance:
The enzyme's mutation has been linked to Diaphyseal medullary stenosis with malignant fibrous histiocytoma, a bone dysplasia leading to poor fracture healing and potential development of aggressive bone sarcoma. Understanding the role of S-methyl-5'-thioadenosine phosphorylase could open doors to potential therapeutic strategies for this condition.