CMAS Inhibitors
CMAS (Cytidine Monophosphate N-Acetylneuraminic Acid Synthetase) plays a pivotal role in the sialylation process, a post-translational modification critical for the proper function of glycoproteins and glycolipids. This enzyme catalyzes the conversion of N-acetylneuraminic acid (Neu5Ac) to its activated form, cytidine monophosphate N-acetylneuraminic acid (CMP-Neu5Ac), which is a crucial donor molecule for sialic acid transferases in the process of sialylation. Sialylation influences a myriad of cellular functions, including cell-cell recognition, signal transduction, and immune response modulation. By regulating the availability of CMP-Neu5Ac, CMAS directly impacts the extent and pattern of sialylation on cell surfaces and secreted proteins, affecting various physiological and pathological processes.
The inhibition of CMAS represents a strategic approach to modulating sialylation patterns on glycoproteins and glycolipids, which can have profound effects on cellular behavior and disease progression. Inhibition can occur through different mechanisms, such as the binding of small molecules to the active site of CMAS, interfering with its ability to convert Neu5Ac to CMP-Neu5Ac. Another approach involves the disruption of the enzyme's interaction with its substrates or cofactors, essential for its catalytic activity. Additionally, allosteric inhibitors can modulate the enzyme's activity by binding to sites other than the active site, inducing conformational changes that reduce its affinity for substrates or its catalytic efficiency. These mechanisms highlight the complexity of inhibiting CMAS activity and the potential for selective intervention in the sialylation pathway. By understanding the nuances of CMAS function and the biochemical basis of its inhibition, researchers can elucidate the role of sialylation in health and disease, offering insights into novel strategies for modulating cellular interactions and functions.
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Siastatin B microbial | 54795-58-3 | sc-215851 | 5 mg | $429.00 | ||
This compound acts as a competitive inhibitor of CMAS by resembling the natural substrate and binding to the enzyme's active site. | ||||||
Zanamivir | 139110-80-8 | sc-208495 | 1 mg | $270.00 | 6 | |
Although primarily an antiviral agent, Zanamivir's structural similarity to sialic acid suggests it can inhibit CMAS by binding to its active site. | ||||||
N-Acetyl-2,3-dehydro-2-deoxyneuraminic acid | 24967-27-9 | sc-215433 sc-215433A sc-215433B | 5 mg 10 mg 25 mg | $168.00 $278.00 $549.00 | ||
N-Acetyl-2,3-dehydro-2-deoxyneuraminic Acid (Neu5Ac2en) is another sialic acid analogue that can bind to the enzyme and inhibit its action. | ||||||
Oseltamivir phosphate | 204255-11-8 | sc-208135 sc-208135A | 10 mg 200 mg | $179.00 $650.00 | 5 | |
Oseltamivir phosphate can inhibit CMAS due to its structural resemblance to sialic acid, potentially blocking the enzyme's active site. | ||||||
(Z)-Pugnac | 132489-69-1 | sc-204415A sc-204415 | 5 mg 10 mg | $224.00 $380.00 | 3 | |
O-(2-Acetamido-2-deoxy-D-glucopyranosylidene)amino N-phenyl carbamate (PUGNAc) is a competitive inhibitor that can bind to the active site of CMAS, preventing substrate access. | ||||||
L-(−)-Fucose | 2438-80-4 | sc-221792 sc-221792A sc-221792B sc-221792C | 10 mg 5 g 50 g 100 g | $31.00 $153.00 $454.00 $840.00 | ||
Fucose is structurally similar to the sugar moieties that interact with CMAS, and can competitively inhibit the enzyme's activity by occupying its active site. | ||||||