![]() D-(+)-Threonine structure
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Common Name | D-(+)-Threonine | ||
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CAS Number | 632-20-2 | 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 | 274ºC | |
MSDS | Chinese USA | Flash Point | 162.9±25.1 °C |
Monitoring neonatal fungal infection with metabolomics.
J. Matern. Fetal. Neonatal. Med. 27 Suppl 2 , 34-8, (2014) The objective of our study was to evaluate the capability of the metabolomics approach to identify the variations of urine metabolites over time related to the neonatal fungal septic condition. The study population included a clinical case of a preterm neonat... |
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Characterization of the xiamenmycin biosynthesis gene cluster in Streptomyces xiamenensis 318.
PLoS ONE 9(6) , e99537, (2014) Xiamenmycin (1) is a prenylated benzopyran derivative with anti-fibrotic activity. To investigate the genetic basis of xiamenmycin biosynthesis, we performed genome mining in the xiamenmycin-producing Streptomyces xiamenensis wild-type strain 318 to identify ... |
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Gene cloning and overproduction of low-specificity D-threonine aldolase from Alcaligenes xylosoxidans and its application for production of a key intermediate for parkinsonism drug.
Appl. Microbiol. Biotechnol. 54 , 44-51, (2000) 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 correspo... |
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Synthesis of beta-hydroxy-alpha-amino acids with a reengineered alanine racemase.
Bioorg. Med. Chem. Lett. 18 , 5987-5990, (2008) 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... |
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L-allo-threonine aldolase from Aeromonas jandaei DK-39: gene cloning, nucleotide sequencing, and identification of the pyridoxal 5'-phosphate-binding lysine residue by site-directed mutagenesis.
J. Bacteriol. 179 , 3555-3560, (1997) 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 ... |
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l-Threonine aldolase, serine hydroxymethyltransferase and fungal alanine racemase. A subgroup of strictly related enzymes specialized for different functions.
Eur. J. Biochem. 268 , 6508-6525, (2001) 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 tetra... |
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Threonine aldolase and alanine racemase: novel examples of convergent evolution in the superfamily of vitamin B6-dependent enzymes.
Biochim. Biophys. Acta 1647 , 214-219, (2003) Vitamin B(6)-dependent enzymes may be grouped into five evolutionarily unrelated families, each having a different fold. Within fold type I enzymes, L-threonine aldolase (L-TA) and fungal alanine racemase (AlaRac) belong to a subgroup of structurally and mech... |
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The crystal structure of D-threonine aldolase from Alcaligenes xylosoxidans provides insight into a metal ion assisted PLP-dependent mechanism.
PLoS ONE 10(4) , e0124056, (2015) Threonine aldolases catalyze the pyridoxal phosphate (PLP) dependent cleavage of threonine into glycine and acetaldehyde and play a major role in the degradation of this amino acid. In nature, L- as well as D-specific enzymes have been identified, but the exa... |