96193-69-0 Usage
Description
D-O-Phospho Threonine, also known as the D enantiomer of Threonine derivative, is a modified amino acid with a phosphoryl group attached to the hydroxyl side chain. It plays a crucial role in various biological processes, including protein phosphorylation and dephosphorylation, which are essential for cell signaling and regulation.
Uses
Used in Pharmaceutical Industry:
D-O-Phospho Threonine is used as a pharmaceutical intermediate for the development of drugs targeting phosphothreonine phosphatases. Its stereoselectivity allows for the design of more specific and potent inhibitors, leading to improved therapeutic outcomes.
Used in Research Applications:
D-O-Phospho Threonine is used as a research tool for studying the role of protein phosphorylation and dephosphorylation in various cellular processes. It helps researchers understand the mechanisms of action and regulation of phosphothreonine phosphatases, which are important for various cellular functions.
Used in Biochemical Assays:
D-O-Phospho Threonine is used as a substrate in biochemical assays to measure the activity of phosphothreonine phosphatases. This allows for the evaluation of enzyme function and the development of potential therapeutic agents targeting these enzymes.
Check Digit Verification of cas no
The CAS Registry Mumber 96193-69-0 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 9,6,1,9 and 3 respectively; the second part has 2 digits, 6 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 96193-69:
(7*9)+(6*6)+(5*1)+(4*9)+(3*3)+(2*6)+(1*9)=170
170 % 10 = 0
So 96193-69-0 is a valid CAS Registry Number.
InChI:InChI=1/C4H10NO6P/c1-2(3(5)4(6)7)11-12(8,9)10/h2-3H,5H2,1H3,(H,6,7)(H2,8,9,10)/t2-,3+/m0/s1
96193-69-0Relevant articles and documents
Optimization of the kinetic resolution of the DL-phospho-monoesters of threonine and serine by random mutagenesis of the acid phosphatase from Salmonella enterica
Van Herk, Teunie,Hartog, Aloysius F.,Ruijssenaars, Harald J.,Kerkman, Richard,Schoemaker, Hans E.,Wever, Ron
, p. 1349 - 1352 (2008/09/16)
Acid phosphatases are enzymes with a broad substrate specificity showing hydrolytic activity towards several different organic phosphate monoesters, such as nucleotides and sugar phosphates. The acid phosphatase from Salmonella enterica ser. typhimurium LT2 (PhoN-Se) is able to hydrolyze O-phospho-DL-threonine to yield L-threonine with a very high enantioselectivity (E > 200). When O-phospho-DL-serine was hydrolyzed by PhoN-Se, D-serine was formed, however, the ee values rapidly dropped to 50 %. Random mutagenesis by error-prone PCR was performed on the phosphatase in order to increase its enantioselectivity in the formation of D-serine. Two variants with increased selectivity from a library of 9600 mutants have been found, N151D and V78L showing E values of 18.1 and 4.1, respectively, compared to 3.4 for the wild-type (WT) enzyme.
