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Fixed Competitive Price Plant Extract - (2S,3R)-2-Amino-3-hydroxybutanoic acid Cas: 72-19-5 99% White crystalline powder – XD BIOCHEM

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Fixed Competitive Price Plant Extract - (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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Fixed Competitive Price Plant Extract - (2S,3R)-2-Amino-3-hydroxybutanoic acid  Cas: 72-19-5  99%  White crystalline powder – XD BIOCHEM detail pictures


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  • Products and services are very good, our leader is very satisfied with this procurement, it is better than we expected,
    5 Stars By Agustin from Paraguay - 2018.05.15 10:52
    This manufacturers not only respected our choice and requirements, but also gave us a lot of good suggestions, ultimately, we successfully completed the procurement tasks.
    5 Stars By Raymond from Mexico - 2018.02.04 14:13
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    Fixed Competitive Price Plant Extract - (2S,3R)-2-Amino-3-hydroxybutanoic acid Cas: 72-19-5 99% White crystalline powder – XD BIOCHEM