Date published: 2026-4-2

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L-allo-Threonine (CAS 28954-12-3)

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Alternate Names:
L(+)-allo-Threonine
CAS Number:
28954-12-3
Molecular Weight:
119.12
Molecular Formula:
C4H9NO3
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.
* Refer to Certificate of Analysis for lot specific data.

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L-allo-Threonine is an isomer of the amino acid threonine, distinguished by the arrangement of its molecular components, which imparts unique properties that have become a focal point in biochemical and structural biology research. Unlike its counterpart, L-threonine, which is incorporated into proteins during translation, L-allo-threonine is not found in proteins and thus serves as a tool for probing protein structure, function, and stability. Researchers leverage L-allo-Threonine in the study of enzyme specificity, exploring how enzymes distinguish between closely related substrates. This isomer also plays a critical role in synthetic biology, where it is used to engineer novel proteins with altered amino acid sequences, enabling the investigation of protein folding mechanisms and the design of proteins with new functions. Additionally, L-allo-Threonine′s unique structural properties make it a valuable component in the development of peptidomimetics, molecules that mimic the structure of peptides and are used to elucidate interactions at the molecular level, offering insights into the fundamental principles of molecular recognition and binding.


L-allo-Threonine (CAS 28954-12-3) References

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  2. Characterization of short-chain dehydrogenase/reductase homologues of Escherichia coli (YdfG) and Saccharomyces cerevisiae (YMR226C).  |  Fujisawa, H., et al. 2003. Biochim Biophys Acta. 1645: 89-94. PMID: 12535615
  3. Towards preparative asymmetric synthesis of beta-hydroxy-alpha-amino acids: L-allo-threonine formation from glycine and acetaldehyde using recombinant GlyA.  |  Makart, S., et al. 2007. J Biotechnol. 130: 402-10. PMID: 17597243
  4. Assessment of threonine metabolism in vivo by gas chromatography/mass spectrometry and stable isotope infusion.  |  Ballèvre, O., et al. 1991. Anal Biochem. 193: 212-9. PMID: 1908193
  5. Discovery and characterization of D-phenylserine deaminase from Arthrobacter sp. TKS1.  |  Muramatsu, H., et al. 2011. Appl Microbiol Biotechnol. 90: 159-72. PMID: 21190106
  6. Alleviation of asthma-related symptoms by a derivative of L-allo threonine.  |  Heo, JC. and Lee, SH. 2013. Int J Mol Med. 31: 881-7. PMID: 23381610
  7. Arg-265: a critical residue of L.donovani cytosolic SHMT in maintaining the binding of THF and catalysis.  |  Gandhi, S., et al. 2015. Exp Parasitol. 149: 16-23. PMID: 25499510
  8. The Important Role of the Hydroxyl Group on the Conformational Adaptability in Bis(l-threoninato)copper(II) Compared to Bis(l-allo-threoninato)copper(II): Quantum Chemical Study.  |  Marković, M., et al. 2016. Inorg Chem. 55: 7694-708. PMID: 27442350
  9. Effect of Novel Compound LX519290, a Derivative of l-allo Threonine, on Antioxidant Potential in Vitro and in Vivo.  |  Chun, K., et al. 2016. Int J Mol Sci. 17: PMID: 27598126
  10. L-Threonine and its analogue added to autoclaved solid medium suppress trichothecene production by Fusarium graminearum.  |  Maeda, K., et al. 2017. Arch Microbiol. 199: 945-952. PMID: 28357472
  11. Biosynthesis of Cyclochlorotine: Identification of the Genes Involved in Oxidative Transformations and Intramolecular O,N-Transacylation.  |  Jiang, Y., et al. 2021. Org Lett. 23: 2616-2620. PMID: 33736433
  12. Terahertz Spectroscopy Study of the Stereoisomers of Threonine.  |  Zeng, R., et al. 2022. Appl Spectrosc. 76: 1132-1141. PMID: 35469427
  13. Interactions between copper (II) ions and L-threonine, L-allo-threonine and L-serine in aqueous solution.  |  Grenouillet, P., et al. 1973. Biochim Biophys Acta. 322: 185-94. PMID: 4765086
  14. Globomycin, a new peptide antibiotic with spheroplast-forming activity. III. Structural determination of globomycin.  |  Nakajima, M., et al. 1978. J Antibiot (Tokyo). 31: 426-32. PMID: 670085
  15. Gene cloning, biochemical characterization and physiological role of a thermostable low-specificity L-threonine aldolase from Escherichia coli.  |  Liu, JQ., et al. 1998. Eur J Biochem. 255: 220-6. PMID: 9692922

Ordering Information

Product NameCatalog #UNITPriceQtyFAVORITES

L-allo-Threonine, 250 mg

sc-255235
250 mg
$281.00