53355-60-5

Basic information

• Product Name: cyclic adenosine-5'-trimetaphosphate
• Synonyms: cyclic adenosine-5'-trimetaphosphate
• CAS NO: 53355-60-5
• Molecular Formula: C₁₀H₁₄N₅O₁₂P₃
• Molecular Weight: 489.1657
• Mol File: 53355-60-5.mol
• Article Data: 3

Chemical Properties

• Boiling Point: 831.4 °C at 760 mmHg
• Flash Point: 456.6 °C
• Appearance: /
• Density: 2.78 g/cm³
• CAS DataBase Reference: cyclic adenosine-5'-trimetaphosphate(CAS DataBase Reference)
• NIST Chemistry Reference: cyclic adenosine-5'-trimetaphosphate(53355-60-5)
• EPA Substance Registry System: cyclic adenosine-5'-trimetaphosphate(53355-60-5)

Safety Data

• Hazardous Substances Data: 53355-60-5(Hazardous Substances Data)

Upstream product

• 58-61-7 adenosine 
• 81926-41-2 adenosine-5'-triphosphate tetrakis-(tetrabutylammonium) salt 
• 34051-17-7 C₁₀H₁₂Cl₂N₅O₅P 

Downstream Products

• 606-67-7 adenosine 5'-triphosphate 
• 1172-42-5 adenosine-5′-diphosphate trisodium salt 
• 56983-23-4 P¹,P⁶-di(adenosine-5') hexaphosphate 
• 5542-28-9 Diadenosine tetraphosphate 
• 41708-91-2 p¹,p⁵-di(adenosine 5'-)pentaphosphate 

Relevant articles and documents

Clickable 5′-γ-Ferrocenyl Adenosine Triphosphate Bioconjugates in Kinase-Catalyzed Phosphorylations

Clickable co-substrate: A tri-functional 5′-γ-ferrocenyl adenosine triphosphate (Fc-ATP) derivative containing a clickable site was synthesized (see figure). This compound is an effective co-substrate in kinase-catalyzed phosphorylation reactions, which can be detected by both electrochemical and immunoassay detection methods. The clickable reaction site makes direct modification possible, which greatly expands its application.

Species- or isozyme-specific enzyme inhibitors. IV. Design of a two-site inhibitor of adenylate kinase with isozyme selectivity

The ATP analogues 6-(n-butylamino)-, 6-(di-n-butylamino)-, and 6-(n-butylthio)-9-β-D-ribofuranosylpurine 5'-triphosphate have been synthesized and studied as inhibitors and/or substrates of the rat muscle adenylate kinase isozyme (AK M) and the rat liver isozymes AK II and III. The 6-NH(n-Bu) and 6-S(n-Bu) analogues were substrates (V(max) relative to ATP, 13-190%) of the three AK isozymes, whereas the 6-N(n-Bu)2 analogue was a weak substrate and a competitive inhibitor of AK M and AK III. The affinities of the analogues relative to ATP [K(M) (ATP)/K(M) or K(i)] were 0.03-0.075 for AK III and 0.14-0.28 for AK M, and affinities for AK M exceeded those for AK III by factors of 2.3-7.0 P1, P6-Di(adenosine-5') pentaphosphate (Ap5A) was synthesized by an improved method and was found to be a potent two-site inhibitor (K(i) = 0.28 μM), competitive toward AMP or ATP, for the three AK isozymes. 8-SEt-Ap5A also behaved as a two-site inhibitor; the 8-SEt group reduced the affinity for AK M 12-fold but increased the affinity for AK II and III 4-fold, resulting in ca. 45-fold more effective inhibition of AK II and III (K(i) = 0.07 μM) than of AK M (K(i) = 3.25 μM). The 8-SEt group of 8-SEt-ATP likewise reduced affinity for the ATP site of AK M but enhanced affinity for the ATP sites of AK II and III, resulting in at least 30-fold more effective inhibition of AK II and III. 8-SEt-AMP inhibited AK II and III noncompetitively (K(i) = 21-24 mM) with respect to AMP, indicating that the 8-(ethylthio) adenosine moiety of 8-SEt-Ap5A probably binds to the ATP sites of these isozymes. 8-SEt-Ap5A had ca. 1000-fold more affinity for AK II or III than did 8-SEt-ATP. The findings indicate that isozyme-selective inhibitory effects of a substrate derivative can be imparted to a two-site inhibitor, leading to significant enhancement of inhibitory potency.