Pseudouridine-5'-monophosphate glycosylase (PUMY)

Pseudouridine-5'-monophosphate glycosylase (PUMY) is an enzyme that catalyzes the second step of the pseudouridine degradation pathway, specifically the cleavage of the C-C glycosidic bond in pseudouridine-5'-monophosphate (ΨMP) to produce uracil and ribose-5-phosphate [1, 5]. This enzyme is unique because it is one of the few known to cleave a C-C glycosidic bond [2, 5]. While pseudouridine is the most abundant modified nucleoside in RNA, its catabolism is essential to prevent the accumulation of ΨMP, which has been shown to be toxic in various organisms, including plants and bacteria [3, 14]. Interestingly, the PUMY enzyme is present in bacteria, fungi, and plants but is notably absent in mammals, including humans [7, 13]. This absence makes it an attractive potential therapeutic target for the development of novel antimicrobial and antifungal agents, as inhibitors could selectively disrupt the metabolism of pathogens without affecting human host cells [7, 11]. Research has shown that compromising PUMY activity in plants leads to severe growth inhibition and germination delays, and similar effects are being explored in fungal pathogens like Candida albicans [3, 11].

Other names

Pseudouridine-5'-phosphate glycosylaseΨMP glycosidasePUMYYeiNPsuGPseudouridine-5'-monophosphate glycosidase

Inhibition of pseudouridine-5'-monophosphate glycosylase leads to the accumulation of toxic pseudouridine-5'-monophosphate (ΨMP), which inhibits growth and development in pathogens [3, 11].