4004-57-3

Usage

Definition

ChEBI: A 3',5'-cyclic pyrimidine nucleotide having uridine as the nucleobase.

InChI:InChI=1/C9H11N2O8P/c12-5-1-2-11(9(14)10-5)8-6(13)7-4(18-8)3-17-20(15,16)19-7/h1-2,4,6-8,13H,3H2,(H,15,16)(H,10,12,14)/t4-,6-,7-,8-/m1/s1

Upstream product

• 110-86-1 pyridine 
• 58-97-9 5'-Uridylic Acid 
• 538-75-0 dicyclohexyl-carbodiimide 
• 63-39-8 UTP 

Downstream Products

• 58-97-9 5'-Uridylic Acid 
• 66-22-8 uracil 
• 84-53-7 uridine-3'-phosphate 
• 131-83-9 uridine 2'-monophosphate 

Relevant academic research and scientific papers

Membrane-permeable octanoyloxybenzyl-masked cNMPs as novel tools for non-invasive cell assays

Adenine nucleotide (AN) 2nd messengers, such as 3',5'-cyclic adenosine monophosphate (cAMP), are central elements of intracellular signaling, but many details of their underlying processes remain elusive. Like all nucleotides, cyclic nucleotide monophosphates (cNMPs) are net-negatively charged at physiologic pH which limits their applicability in cell-based settings. Thus, many cellular assays rely on sophisticated techniques like microinjection or electroporation. This setup is not feasible for medium- to high-throughput formats, and the mechanic stress that cells are exposed to raises the probability of interfering artefacts or false-positives. Here, we present a short and flexible chemical route yielding membrane-permeable, bio-reversibly masked cNMPs for which we employed the octanoyloxybenzyl (OB) group. We further show hydrolysis studies on chemical stability and enzymatic activation, and present results of real-time assays, where we used cAMP and Ca2+ live cell imaging to demonstrate high permeability and prompt intracellular conversion of some selected masked cNMPs. Based on these results, our novel OB-masked cNMPs constitute valuable precursor-tools for non-invasive studies on intracellular signaling.

Cytidylyl and uridylyl cyclase activity of bacillus anthracis edema factor and bordetella pertussis CyaA

Cyclic adenosine 3′,5′-monophosphate (cAMP) and cyclic guanosine 3′,5′-monophosphate (cGMP) are second messengers for numerous mammalian cell functions. The natural occurrence and synthesis of a third cyclic nucleotide (cNMP), cyclic cytidine 3′,5′-monophosphate (cCMP), is a matter of controversy, and almost nothing is known about cyclic uridine 3′,5′-monophosphate (cUMP). Bacillus anthracis and Bordetella pertussis secrete the adenylyl cyclase (AC) toxins edema factor (EF) and CyaA, respectively, weakening immune responses and facilitating bacterial proliferation. A cell-permeable cCMP analogue inhibits human neutrophil superoxide production. Here, we report that EF and CyaA also possess cytidylyl cyclase (CC) and uridylyl cyclase (UC) activity. CC and UC activity was determined by a radiometric assay, using [α-32P]CTP and [α-32P]UTP as substrates, respectively, and by a high-performance liquid chromatography method. The identity of cNMPs was confirmed by mass spectrometry. On the basis of available crystal structures, we developed a model illustrating conversion of CTP to cCMP by bacterial toxins. In conclusion, we have shown both EF and CyaA have a rather broad substrate specificity and exhibit cytidylyl and uridylyl cyclase activity. Both cCMP and cUMP may contribute to toxin actions.