D-Threonine is sweet[1] and toxic in nature.[2]It acts as an inhibitor of L-threonine dehydratase.[3]
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.[4]
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
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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
Journal of bacteriology, 179(11), 3555-3560 (1997-06-01)
We have isolated the gene encoding L-allo-threonine aldolase (L-allo-TA) from Aeromonas jandaei DK-39, a pyridoxal 5'-phosphate (PLP)-dependent enzyme that stereospecifically catalyzes the interconversion of L-allo-threonine and glycine. The gene contains an open reading frame consisting of 1,014 nucleotides corresponding to
Applied microbiology and biotechnology, 54(1), 44-51 (2000-08-22)
The dtaAX gene encoding a pyridoxal 5'-phosphate (pyridoxal-P)-dependent low-specificity D-threonine aldolase was cloned from the chromosomal DNA of Alcaligenes xylosoxidans IFO 12669. It contains an open reading frame consisting of 1,134 nucleotides corresponding to 377 amino acid residues. The predicted
Fishmeal with different levels of biogenic amines in aquafeed: Comparison of feed protein quality, fish growth performance, and metabolism
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