76742-18-2 Usage
Description
Cytidine 5'-PhosphoroMorpholidate N,N'-Dicyclohexyl-4-MorpholinecarboxiMidaMide is a chemical compound that serves as an intermediate in the preparation of Citicoline (C508050), a naturally occurring nucleotide. It is characterized by its off-white solid appearance.
Uses
Used in Pharmaceutical Industry:
Cytidine 5'-PhosphoroMorpholidate N,N'-Dicyclohexyl-4-MorpholinecarboxiMidaMide is used as an intermediate for the synthesis of Citicoline, which is a naturally occurring nucleotide. This application is significant because Citicoline plays a crucial role in various physiological processes and has potential therapeutic applications in the treatment of cognitive disorders and other conditions related to brain function.
Used in Chemical Synthesis:
In the field of chemical synthesis, Cytidine 5'-PhosphoroMorpholidate N,N'-Dicyclohexyl-4-MorpholinecarboxiMidaMide is utilized as a key compound in the preparation of other nucleotides and related molecules. Its unique structure and reactivity make it a valuable building block for the development of new pharmaceuticals and other bioactive compounds.
Check Digit Verification of cas no
The CAS Registry Mumber 76742-18-2 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 7,6,7,4 and 2 respectively; the second part has 2 digits, 1 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 76742-18:
(7*7)+(6*6)+(5*7)+(4*4)+(3*2)+(2*1)+(1*8)=152
152 % 10 = 2
So 76742-18-2 is a valid CAS Registry Number.
76742-18-2Relevant articles and documents
Covalent Protein Labeling by Enzymatic Phosphocholination
Heller, Katharina,Ochtrop, Philipp,Albers, Michael F.,Zauner, Florian B.,Itzen, Aymelt,Hedberg, Christian
supporting information, p. 10327 - 10330 (2015/09/01)
We present a new protein labeling method based on the covalent enzymatic phosphocholination of a specific octapeptide amino acid sequence in intact proteins. The bacterial enzyme AnkX from Legionella pneumophila has been established to transfer functional phosphocholine moieties from synthetically produced CDP-choline derivatives to N-termini, C-termini, and internal loop regions in proteins of interest. Furthermore, the covalent modification can be hydrolytically removed by the action of the Legionella enzyme Lem3. Only a short peptide sequence (eight amino acids) is required for efficient protein labeling and a small linker group (PEG-phosphocholine) is introduced to attach the conjugated cargo.
