1981-49-3

Usage

Uses

Used in Pharmaceutical Industry:
(2-hydroxy-3-phosphonooxy-propanoyl)oxyphosphonic acid is used as a therapeutic agent for its potential role in oncogenesis. It can be employed in the development of drugs that target cancer cells by interfering with the metabolic pathways involved in tumor growth and progression.
Used in Research and Development:
In the field of biomedical research, (2-hydroxy-3-phosphonooxy-propanoyl)oxyphosphonic acid serves as an important compound for studying the metabolic pathways associated with cancer. It can be utilized in the design and synthesis of novel molecules with potential anticancer properties, as well as in the investigation of the underlying mechanisms of oncogenesis.
Used in Drug Delivery Systems:
Similar to gallotannin, (2-hydroxy-3-phosphonooxy-propanoyl)oxyphosphonic acid can also be incorporated into drug delivery systems to enhance its bioavailability and therapeutic efficacy. By employing various organic and metallic nanoparticles as carriers, the compound can be more effectively delivered to cancer cells, improving its overall impact on tumor growth inhibition and cancer treatment.

InChI:InChI=1/C3H8O10P2/c4-2(1-12-14(6,7)8)3(5)13-15(9,10)11/h2,4H,1H2,(H2,6,7,8)(H2,9,10,11)

Upstream product

• 142-10-9 DL-glyceraldehyde 3-phosphate 
• 820-11-1 3-phosphoglyceric acid 
• 24027-80-3 2',3'-dideoxyadenosine 5'-triphosphate 
• 68726-28-3 2',3'-dideoxyguanosine-5'-triphosphate 
• 66341-18-2 Acyclovir triphosphate 
• 13191-15-6 β-L-CTP 
• 65-47-4 cytidine triphosphate 
• 365-08-2 dTTP 
• 63-39-8 UTP 
• 1927-31-7 dATP 
• 591-57-1 D-glyceraldehyde-3-phosphate 
• 86-01-1 Guanosine 5'-triphosphate 
• 2564-35-4 2'-deoxyguanosine 5'-triphosphate 
• 56-65-5 ATP 

Downstream Products

• 820-11-1 3-phosphoglyceric acid 
• 56-65-5 ATP 

Relevant academic research and scientific papers

carba Nicotinamide Adenine Dinucleotide Phosphate: Robust Cofactor for Redox Biocatalysis

Here we report a new robust nicotinamide dinucleotide phosphate cofactor analog (carba-NADP+) and its acceptance by many enzymes in the class of oxidoreductases. Replacing one ribose oxygen with a methylene group of the natural NADP+ was found to enhance stability dramatically. Decomposition experiments at moderate and high temperatures with the cofactors showed a drastic increase in half-life time at elevated temperatures since it significantly disfavors hydrolysis of the pyridinium-N?glycoside bond. Overall, more than 27 different oxidoreductases were successfully tested, and a thorough analytical characterization and comparison is given. The cofactor carba-NADP+ opens up the field of redox-biocatalysis under harsh conditions.

Kinetic and mechanistic characterization of the glyceraldehyde 3-phosphate dehydrogenase from Mycobacterium tuberculosis

Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is a glycolytic protein responsible for the conversion of glyceraldehyde 3-phosphate (G3P), inorganic phosphate and nicotinamide adenine dinucleotide (NAD+) to 1,3-bisphosphoglycerate (1,3-BPG) and the reduced form of nicotinamide adenine dinucleotide (NADH). Here we report the characterization of GAPDH from Mycobacterium tuberculosis (Mtb). This enzyme exhibits a kinetic mechanism in which first NAD+, then G3P bind to the active site resulting in the formation of a covalently bound thiohemiacetal intermediate. After oxidation of the thiohemiacetal and subsequent nucleotide exchange (NADH off, NAD+ on), the binding of inorganic phosphate and phosphorolysis yields the product 1,3-BPG. Mutagenesis and iodoacetamide (IAM) inactivation studies reveal the conserved C158 to be responsible for nucleophilic catalysis and that the conserved H185 to act as a catalytic base. Primary, solvent and multiple kinetic isotope effects revealed that the first half-reaction is rate limiting and utilizes a step-wise mechanism for thiohemiacetal oxidation via a transient alkoxide to promote hydride transfer and thioester formation.

Broad specificity of human phosphoglycerate kinase for antiviral nucleoside analogs

Nucleoside analogs used in antiviral therapies need to be phosphorylated to their tri-phospho counterparts in order to be active on their cellular target. Human phosphoglycerate kinase (hPGK) was recently reported to participate in the last step of phosphorylation of cytidine l-nucleotide derivatives [Krishnan PGE, Lam W, Dutschman GE, Grill SP, Cheng YC. Novel role of 3-phosphoglycerate kinase, a glycolytic enzyme, in the activation of l-nucleoside analogs, a new class of anticancer and antiviral agents. J Biol Chem 2003;278:36726-32]. In the present work, we extended the enzymatic study of human PGK specificity to purine and pyrimidine nucleotide derivatives in both d- and l-configuration. Human PGK demonstrated catalytic efficiencies in the 104-10 5 M-1 s-1 range for purine ribo-, deoxyribo- and dideoxyribonucleotide derivatives, either in d- or l-configuration. In contrast, it was poorly active with natural pyrimidine d-nucleotides (less than 103 M-1 s-1). Pyrimidine l-enantiomers, which are promising therapeutic analogs against B hepatitis, were 2-25 times better substrates than their d-counterparts. The broad specificity of substrate of human PGK suggests that this enzyme may be involved in the cellular activation of several antiviral nucleoside analogs including dideoxyinosine, acyclovir, l-2′-deoxycytosine and l-2′-deoxythymidine.