T8250
D-Threonine
≥98% (TLC), suitable for UHPLC
Synonym(s):
(2R,3S)-2-Amino-3-hydroxybutyric acid, D-α-Amino-β-hydroxybutyric acid
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About This Item
Empirical Formula (Hill Notation):
C4H9NO3
CAS Number:
Molecular Weight:
119.12
Beilstein:
1721643
EC Number:
MDL number:
UNSPSC Code:
12352209
PubChem Substance ID:
NACRES:
NA.26
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Product Name
D-Threonine, ≥98% (TLC)
Quality Level
Assay
≥98% (TLC)
form
powder or crystals
technique(s)
UHPLC: suitable
color
white
mp
274 °C
solubility
H2O: soluble
SMILES string
C[C@H](O)[C@@H](N)C(O)=O
InChI
1S/C4H9NO3/c1-2(6)3(5)4(7)8/h2-3,6H,5H2,1H3,(H,7,8)/t2-,3+/m0/s1
InChI key
AYFVYJQAPQTCCC-STHAYSLISA-N
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General description
D-Threonine is sweet and toxic in nature.It acts as an inhibitor of L-threonine dehydratase.
Application
D-Threonine has been used as a constituent of standard mix in Ultra-high performance liquid chromatography (UHPLC) system for quantification of amino acid racemization.
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Fishmeal with different levels of biogenic amines in aquafeed: Comparison of feed protein quality, fish growth performance, and metabolism
Jasour M, et al.
Aquaculture (Amsterdam, Netherlands), 488, 80-89 (2018)
Test, 244 (1969)
Kateryna Fesko et al.
Bioorganic & medicinal chemistry letters, 18(22), 5987-5990 (2008-09-02)
The Y265A mutant of alanine racemase (alrY265A) was evaluated as a catalyst for the synthesis of beta-hydroxy-alpha-amino acids. It promotes the PLP-dependent aldol condensation of glycine with a range of aromatic aldehydes. The desired products were obtained with complete stereocontrol
Alessandro Paiardini et al.
Biochimica et biophysica acta, 1647(1-2), 214-219 (2003-04-11)
Vitamin B(6)-dependent enzymes may be grouped into five evolutionarily unrelated families, each having a different fold. Within fold type I enzymes, L-threonine aldolase (L-TA) and fungal alanine racemase (AlaRac) belong to a subgroup of structurally and mechanistically closely related proteins
The Journal of Biological Chemistry, 244 (1969)
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