1110-99-2

Basic information

• Product Name: [(2R,3S,4R,5R)-5-[6-amino-1-[(2R,3R,4S,5R)-3,4-dihydroxy-5-(phosphonooxymethyl)tetrahydrofuran-2-yl]-2H-purin-9-yl]-3,4-dihydroxy-tetrahydrofuran-2-yl]methyl (hydroxy-phosphonooxy-phosphoryl) hydrogen phosphate
• CAS NO: 1110-99-2
• Molecular Formula: C₁₅H₂₇N₅O₂₀P₄
• Molecular Weight: 721.2914
• Mol File: 1110-99-2.mol
• Article Data: 1

Chemical Properties

• Boiling Point: 1046.8°C at 760 mmHg
• Flash Point: 586.9°C
• Density: 2.67g/cm³
• Vapor Pressure: 0mmHg at 25°C
• Refractive Index: 1.897
• CAS DataBase Reference: [(2R,3S,4R,5R)-5-[6-amino-1-[(2R,3R,4S,5R)-3,4-dihydroxy-5-(phosphonooxymethyl)tetrahydrofuran-2-yl]-2H-purin-9-yl]-3,4-dihydroxy-tetrahydrofuran-2-yl]methyl (hydroxy-phosphonooxy-phosphoryl) hydrogen phosphate(CAS DataBase Reference)
• NIST Chemistry Reference: [(2R,3S,4R,5R)-5-[6-amino-1-[(2R,3R,4S,5R)-3,4-dihydroxy-5-(phosphonooxymethyl)tetrahydrofuran-2-yl]-2H-purin-9-yl]-3,4-dihydroxy-tetrahydrofuran-2-yl]methyl (hydroxy-phosphonooxy-phosphoryl) hydrogen phosphate(1110-99-2)
• EPA Substance Registry System: [(2R,3S,4R,5R)-5-[6-amino-1-[(2R,3R,4S,5R)-3,4-dihydroxy-5-(phosphonooxymethyl)tetrahydrofuran-2-yl]-2H-purin-9-yl]-3,4-dihydroxy-tetrahydrofuran-2-yl]methyl (hydroxy-phosphonooxy-phosphoryl) hydrogen phosphate(1110-99-2)

Safety Data

• Hazardous Substances Data: 1110-99-2(Hazardous Substances Data)

Upstream product

• 97-55-2 5-phosphoribosyl-1-pyrophosphate 
• 56-65-5 ATP 

Downstream Products

• 119340-53-3 cyclic adenosine 5'-diphosphate ribose 

Relevant articles and documents

Campylobacter jejuni adenosine triphosphate phosphoribosyltransferase is an active hexamer that is allosterically controlled by the twisting of a regulatory tail

Adenosine triphosphate phosphoribosyltransferase (ATP-PRT) catalyzes the first committed step of the histidine biosynthesis in plants and microorganisms. Here, we present the functional and structural characterization of the ATP-PRT from the pathogenic ε-proteobacteria Campylobacter jejuni (CjeATP-PRT). This enzyme is a member of the long form (HisGL) ATP-PRT and is allosterically inhibited by histidine, which binds to a remote regulatory domain, and competitively inhibited by AMP. In the crystalline form, CjeATP-PRT was found to adopt two distinctly different hexameric conformations, with an open homohexameric structure observed in the presence of substrate ATP, and a more compact closed form present when inhibitor histidine is bound. CjeATP-PRT was observed to adopt only a hexameric quaternary structure in solution, contradicting previous hypotheses favoring an allosteric mechanism driven by an oligomer equilibrium. Instead, this study supports the conclusion that the ATP-PRT long form hexamer is the active species; the tightening of this structure in response to remote histidine binding results in an inhibited enzyme.