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T8250

Sigma-Aldrich

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:
632-20-2
Molecular Weight:
119.12
Beilstein:
1721643
EC Number:
211-171-8
MDL number:
MFCD00064269
UNSPSC Code:
12352209
PubChem Substance ID:
24900513
NACRES:
NA.26

product name

D-Threonine, ≥98% (TLC)

Quality Level

200

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.

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Test, 244 (1969)
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)
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
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R Contestabile et al.
European journal of biochemistry, 268(24), 6508-6525 (2001-12-12)
Serine hydroxymethyltransferase (SHMT) is a member of the fold type I family of vitamin B6-dependent enzymes, a group of evolutionarily related proteins that share the same overall fold. The reaction catalysed by SHMT, the transfer of Cbeta of serine to
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