17885-08-4 Usage
Description
O-PHOSPHO-L-SERINE, also known as DL-O-Phosphoserine, is a serine derivative that features a phosphono group substitution at the oxygen atom of serine. It is a white to faint beige crystalline powder with unique chemical properties that make it valuable in various applications.
Uses
Used in Biochemical Research:
O-PHOSPHO-L-SERINE is used as a biochemical research compound for studying alternative pathways in the biosynthesis of cysteine and selenocysteine. Its unique structure allows researchers to explore its role in these processes and potentially develop new methods for synthesizing these essential amino acids.
Used in Pharmaceutical Industry:
In the pharmaceutical industry, O-PHOSPHO-L-SERINE is used as an intermediate in the synthesis of various drugs and pharmaceutical compounds. Its unique chemical properties make it a valuable building block for the development of new medications with potential therapeutic applications.
Used in Nutritional Supplements:
O-PHOSPHO-L-SERINE may also be used as an ingredient in nutritional supplements, particularly those aimed at supporting the synthesis of essential amino acids and promoting overall health and well-being.
Biochem/physiol Actions
O-Phospho-DL-serine (pSer) is used in the study of non-enzymatic aminophospholipid glycation.
Check Digit Verification of cas no
The CAS Registry Mumber 17885-08-4 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,7,8,8 and 5 respectively; the second part has 2 digits, 0 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 17885-08:
(7*1)+(6*7)+(5*8)+(4*8)+(3*5)+(2*0)+(1*8)=144
144 % 10 = 4
So 17885-08-4 is a valid CAS Registry Number.
InChI:InChI=1/C3H8NO6P.H2O/c4-2(3(5)6)1-10-11(7,8)9;/h2H,1,4H2,(H,5,6)(H2,7,8,9);1H2/t2-;/m0./s1
17885-08-4Relevant articles and documents
Understanding non-enzymatic aminophospholipid glycation and its inhibition. Polar head features affect the kinetics of Schiff base formation
Caldes, Catalina,Vilanova, Bartolome,Adrover, Miquel,Munoz, Francisco,Donoso, Josefa
experimental part, p. 4536 - 4543 (2011/09/19)
Non-enzymatic aminophospholipid glycation is an especially important process because it alters the stability of lipid bilayers and interferes with cell function and integrity as a result. However, the kinetic mechanism behind this process has scarcely been studied. As in protein glycation, the process has been suggested to involve the formation of a Schiff base as the initial, rate-determining step. In this work, we conducted a comparative kinetic study of Schiff base formation under physiological conditions in three low-molecular weight analogues of polar heads in the naturally occurring aminophospholipids O-phosphorylethanolamine (PEA), O-phospho-dl-serine (PSer) and 2-aminoethylphenethylphosphate (APP) with various glycating carbonyl compounds (glucose, arabinose and acetol) and the lipid glycation inhibitor pyridoxal 5′-phosphate (PLP). Based on the results, the presence of a phosphate group and a carboxyl group in α position respect to the amino group decrease the formation constant for the Schiff base relative to amino acids. On the other hand, esterifying the phosphate group with a non-polar substituent in APP increases the stability of its Schiff base. The observed kinetic formation constants of aminophosphates with carbonyl groups were smaller than those for PLP. Our results constitute an important contribution to understanding the competitive inhibition effect of PLP on aminophospholipid glycation.
