3913-50-6 Usage
Description
3-HYDROXY-2,2-DIMETHOXY-PROPANOIC ACID 3-PHOSPHATE TRI(CYCLOHEXYLAMMONIUM) SALT, also known as ChEBI, is a carboxyalkyl phosphate derivative of pyruvic acid with a 3-phosphonooxy group substitution at position 3. 3-HYDROXY-2,2-DIMETHOXY-PROPANOIC ACID 3-PHOSPHATE TRI(CYCLOHEXYLAMMONIUM) SALT plays a significant role in the activation of ATF through its involvement in mTORC1 signaling pathways.
Uses
Used in Pharmaceutical Industry:
3-HYDROXY-2,2-DIMETHOXY-PROPANOIC ACID 3-PHOSPHATE TRI(CYCLOHEXYLAMMONIUM) SALT is used as a key compound in the preparation of mTORC1 signaling agents for the activation of ATF. Its role in this process is crucial for the development of potential therapeutic agents targeting various diseases and conditions related to the mTORC1 signaling pathway.
Used in Research and Development:
In the field of research and development, 3-HYDROXY-2,2-DIMETHOXY-PROPANOIC ACID 3-PHOSPHATE TRI(CYCLOHEXYLAMMONIUM) SALT serves as an essential tool for studying the mechanisms and functions of mTORC1 signaling and its regulation by ATF. This knowledge can be applied to develop novel therapeutic strategies and improve our understanding of the underlying molecular processes in various diseases.
Check Digit Verification of cas no
The CAS Registry Mumber 3913-50-6 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 3,9,1 and 3 respectively; the second part has 2 digits, 5 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 3913-50:
(6*3)+(5*9)+(4*1)+(3*3)+(2*5)+(1*0)=86
86 % 10 = 6
So 3913-50-6 is a valid CAS Registry Number.
InChI:InChI=1/C3H5O7P/c4-1(2(5)6)3(7)11(8,9)10/h3,7H,(H,5,6)(H2,8,9,10)
3913-50-6Relevant articles and documents
Crystal structures and kinetics of Type III 3-phosphoglycerate dehydrogenase reveal catalysis by lysine
Singh, Rohit K.,Raj, Isha,Pujari, Rajesh,Gourinath, Samudrala
, p. 5498 - 5512 (2015/02/19)
D-Phosphoglycerate dehydrogenase (PGDH) catalyzes the first committed step of the phosphorylated serine biosynthesis pathway. Here, we report for the first time, the crystal structures of Type IIIK PGDH from Entamoeba histolytica in the apo form, as well as in complexes with substrate (3-phosphoglyceric acid) and cofactor (NAD+) to 2.45, 1.8 and 2.2 A resolution, respectively. Comparison of the apo structure with the substrate-bound structure shows that the substrate-binding domain is rotated by ~ 20° to close the active-site cleft. The cofactor-bound structure also shows a closed-cleft conformation, in which NAD+ is bound to the nucleotide-binding domain and a formate ion occupies the substrate-binding site. Superposition of the substrate- and cofactor-bound structures represents a snapshot of the enzyme in the active form, where C2 of the substrate and C4N of the cofactor are 2.2 A apart, and the amino group of Lys263 is close enough to the substrate to remove the proton from the hydroxyl group of PGA, indicating the role of Lys in the catalysis. Mutation of Lys263 to Ala yields just 0.8% of the specific activity of the wild-type enzyme, revealing that Lys263 indeed plays an integral role in the catalytic activity. The detectable activity of the mutant, however, indicates that after 20° rotation of the substrate-binding domain, the resulting positions of the substrate and cofactor are sufficiently close to make a productive reaction.