D-(+)-Threonine
D-(+)-Threonine structure
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Common Name | D-(+)-Threonine | ||
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| CAS Number | 144-98-9 | Molecular Weight | 119.119 | |
| Density | 1.3±0.1 g/cm3 | Boiling Point | 345.8±32.0 °C at 760 mmHg | |
| Molecular Formula | C4H9NO3 | Melting Point | 256ºC | |
| MSDS | USA | Flash Point | 162.9±25.1 °C | |
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Influence of Free Amino Acids, Oligopeptides, and Polypeptides on the Formation of Pyrazines in Maillard Model Systems.
J. Agric. Food Chem. 63 , 5364-72, (2015) Pyrazines are specific Maillard reaction compounds known to contribute to the unique aroma of many products. Most studies concerning the generation of pyrazines in the Maillard reaction have focused on amino acids, while little information is available on the... |
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Threonine aldolases-screening, properties and applications in the synthesis of non-proteinogenic beta-hydroxy-alpha-amino acids.
Appl. Microbiol. Biotechnol. 88 , 409-424, (2010) Threonine aldolases (TAs) constitute a powerful tool for catalyzing carbon-carbon bond formations in synthetic organic chemistry, thus enabling an enantio- and diastereoselective synthesis of beta-hydroxy-alpha-amino acids. Starting from the achiral precursor... |
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Importance of tyrosine residues of Bacillus stearothermophilus serine hydroxymethyltransferase in cofactor binding and L-allo-Thr cleavage.
FEBS J. 275 , 4606-4619, (2008) Serine hydroxymethyltransferase (SHMT) from Bacillus stearothermophilus (bsSHMT) is a pyridoxal 5'-phosphate-dependent enzyme that catalyses the conversion of L-serine and tetrahydrofolate to glycine and 5,10-methylene tetrahydrofolate. In addition, the enzym... |
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Discovery and characterization of D-phenylserine deaminase from Arthrobacter sp. TKS1.
Appl. Microbiol. Biotechnol. 90 , 159-172, (2011) We discovered a D-phenylserine deaminase that catalyzed the pyridoxal 5'-phosphate (PLP)-dependent deamination reaction from D-threo-phenylserine to phenylpyruvate in newly isolated Arthrobacter sp. TKS1. The enzyme was partially purified, and its N-terminal ... |