632-20-2
632-20-2
Chemical Structure
D-Threonine
Synonym(s): H-D-Thr-OH
- CAS No.: 632-20-2
- Formula:C4H9NO3
- Molecular Weight:119.12
IUPAC Name: D-threonine
InChIKey: AYFVYJQAPQTCCC-STHAYSLISA-N
SMILES: OC([C@@H]([C@@H](O)C)N)=O
Biological Activity: D-Threonine (H-D-Thr-OH) is an important non-natural amino acid. D-Threonine serves as a chiral building block for the asymmetric synthesis of compounds. D-Threonine is a metabolite of Saccharomyces cerevisiae. D-Threonine is cleaved into glycine and acetaldehyde under the catalysis of D-threonine aldolase[1][2][3].
| Cat. No. | Product Name | Purity | Description | Pricing | |||||||||||||||||||
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D-Threonine | 99.40% | D-Threonine (H-D-Thr-OH) is an important non-natural amino acid. D-Threonine serves as a chiral building block for the asymmetric synthesis of compounds. D-Threonine is a metabolite of Saccharomyces cerevisiae. D-Threonine is cleaved into glycine and acetaldehyde under the catalysis of D-threonine aldolase. | ||||||||||||||||||||
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D-Threonine-d2 | D-Threonine-d2 (H-D-Thr-OH-d2) is the deuterium labeled D-Threonine (HY-W012874). D-Threonine (H-D-Thr-OH) is an important non-natural amino acid. D-Threonine serves as a chiral building block for the asymmetric synthesis of compounds. D-Threonine is a metabolite of Saccharomyces cerevisiae. D-Threonine is cleaved into glycine and acetaldehyde under the catalysis of D-threonine aldolase. | |||||||||||||||||||||
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Structural Analogs
-
Similarity Score 1.00
HY-N0658L-Threonine -
Similarity Score 1.00
HY-N0658ARDL-Threonine (Standard) -
Similarity Score 1.00
HY-N0658SL-Threonine-15N -
Similarity Score 1.00
HY-N0658S3L-Threonine-13C4,15N -
Similarity Score 1.00
HY-N0658S6L-Threonine-13C4 -
Similarity Score 1.00
HY-W001959RD-Allothreonine (Standard) -
Similarity Score 1.00
HY-W008315RL-Allothreonine (Standard) -
Similarity Score 1.00
HY-W102335(Rac)-Threonine -
Similarity Score 0.89
HY-N68584-Hydroxyisoleucine -
Explore the MedChemAI to find more analogs
References
- [1]. Ito T, et al. Enzymatic assay of D-serine using D-serine dehydratase from Saccharomyces cerevisiae. Anal Biochem. 2007 Dec 15;371(2):167-72. [Content Brief]
- [2]. Kataoka M, et al. Isolation and characterization of D-threonine aldolase, a pyridoxal-5'-phosphate-dependent enzyme from Arthrobacter sp. DK-38. Eur J Biochem. 1997 Sep 1;248(2):385-93. [Content Brief]
- [3]. Han SW, Shin JS. Preparation of D-threonine by biocatalytic kinetic resolution. Journal of Molecular Catalysis B: Enzymatic. 2015 Dec 1;122:227-32.
