96193-69-0

Usage

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.

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

Upstream product

• 80-68-2 DL-threonine 
• 1114-81-4 O-phospho-DL-threonine 

Downstream Products

• 600-18-0 2-Oxobutyric acid 
• 86119-84-8 phosphoric acid 
• 72-19-5 L-threonine 
• 632-20-2 D-Threonine 

Relevant academic research and scientific papers

Optimization of the kinetic resolution of the DL-phospho-monoesters of threonine and serine by random mutagenesis of the acid phosphatase from Salmonella enterica

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.

Enzymatic synthesis of β-hydroxy-α-amino acids based on recombinant D- and L-threonine aldolases

To exploit the enzymatic method for the synthesis of β-hydroxy-α-amino acids, the genes coding for the Escherichia coli L-threonine aldolase (LTA; EC 2.1.2.1) and Xanthomonus oryzae D-threonine aldolase (DTA) were cloned and overexpressed in E. coli through primer-directed polymerase chain reactions. The purified recombinant enzymes were studied with respect to kinetics, specificity, stability, additive requirement, temperature profile, and pH dependency. DTA requires magnesium ion as a cofactor, while LTA needs no metal ions. These enzymes work well in the presence of DMSO with concentration up to 40%, and DMSO-induced rate acceleration of LTA-catalyzed reaction was observed. Both enzymes use pyridoxal phosphate coenzyme to activate glycine to react with a wide range of aldehydes. LTA gave erythro-β-hydroxy-α-L-amino acids with aliphatic aldehydes and the threo isomer with aromatic aldehydes as kinetically controlled products. On the other hand, DTA formed threo-β-hydroxy-α-D-amino acids as kinetically controlled products with aliphatic and aromatic aldehydes but the diastereoselectivity was lower than that of LTA. Under optimal conditions, several β-hydroxy-α-amino acid derivatives (3-hydroxyleucines, γ-benzyloxythreonines, γ-benzyloxymethylthreonines, and poplyoxamic acids) have been stereoselectively synthesized on preparative scales using these enzymes. Also, the tandem use of DTA and phosphatases has made possible the synthesis and separation of D-allo-threonine phosphate and D-threonine.