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Factory source Pharmaceutical Manager - (2S,3R)-2-Amino-3-hydroxybutanoic acid Cas: 72-19-5 99% White crystalline powder – XD BIOCHEM

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Factory source Pharmaceutical Manager - (2S,3R)-2-Amino-3-hydroxybutanoic acid Cas: 72-19-5 99% White crystalline powder – XD BIOCHEM Detail:

Catalog Number XD90285
Product Name (2S,3R)-2-Amino-3-hydroxybutanoic acid

CAS

72-19-5

Molecular Formula

C4H9NO3

Molecular Weight

119.11916
Storage Details Ambient

Harmonized Tariff Code

29225000

 

Product Specification

Assay 99 – 101%
Appearance White crystalline powder
Specific rotation -27.5 to -29.0
Heavy metals 10ppm Max.
AS 10ppm max
pH 5.2 – 6.5
SO4 <0.020%
Fe 10ppm max
Loss on Drying <0.20%
Residue on Ignition <0.10%
Transmittance NLT 98%
Cl <0.02%
Ammonium salt <0.02%

 

Serine/threonine protein phosphatases have been described in many pathogenic bacteria as essential enzymes involved in phosphorylation-dependent signal transduction pathways and frequently associated with the virulence of these organisms. An inspection of Mycoplasma synoviae genome revealed the presence of a gene (prpC) encoding a putative protein phosphatase of the protein phosphatase 2C (PP2C) subfamily. Here, we report a complete biochemical characterization of M. synoviae phosphatase (PrpC) and the particular role of metal ions in the structure-function relationship of this enzyme. PrpC amino acid sequence analysis revealed that all the residues involved in the dinuclear metal center and the putative third metal ion-coordinating residues, conserved in PP2C phosphatases, are present in PrpC. PrpC is a monomeric protein able to dephosphorylate phospho-substrates with Mn(2+) ions’ dependence. Thermal stability analysis demonstrated the enzyme stability at mild temperatures and the inf luence of Mn(2+) ions in this property. Mass spectrometry analysis suggested that three metal ions bind to PrpC, two of which with an apparent high-affinity constant. Mutational analysis of the putative third metal-coordinating residues, Asp122 and Arg164, revealed that these variants exhibited a weaker binding of manganese ions, and that both mutations affected PrpC phosphatase activity. According to these results, PrpC is a metal-dependent protein phosphatase member with an improved stability in the holo form and with Asp122, possibly implicated in the third metal-binding site, essential to catalytic activity.


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With state-of-the-art technologies and facilities, strict good quality regulate, reasonable cost, exceptional assistance and close co-operation with prospects, we're devoted to supplying the top benefit for our customers for Factory source Pharmaceutical Manager - (2S,3R)-2-Amino-3-hydroxybutanoic acid Cas: 72-19-5 99% White crystalline powder – XD BIOCHEM , The product will supply to all over the world, such as: Madras, United Kingdom, Poland, With the goal of "zero defect". To care for the environment, and social returns, care employee social responsibility as own duty. We welcome friends from all over the world to visit and guide us so that we can achieve the win-win goal together.
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    Factory source Pharmaceutical Manager - (2S,3R)-2-Amino-3-hydroxybutanoic acid Cas: 72-19-5 99% White crystalline powder – XD BIOCHEM