Disease relevance of NSC 46702

• Taken together, low specificity D-threonine aldolase from Arthrobacter sp. strain DK-38, with a unique primary structure, is a novel metal-activated pyridoxal enzyme [1].
• NADP(+)-dependent D-threonine dehydrogenase from Pseudomonas cruciviae IFO 12047 [2].
• Stereochemistry of the conversions of L-threonine and D-threonine into 2-oxobutanoate by the L-threonine and D-threonine dehydratases of Serratia marcescens [3].
• The predicted amino acid sequence displayed 35% and 22% identity with that of the D-threonine aldolase of Arthrobacter sp. DK-38 and Alcaligenes xylosoxidan IFO 12669, respectively [4].
• The recombinant low-specificity D-threonine aldolase was shown to be an efficient biocatalyst for resolution of L-beta-3,4-methylenedioxyphenylserine, an intermediate for production of a therapeutic drug for Parkinson's disease [5].

High impact information on NSC 46702

• A novel metal-activated pyridoxal enzyme with a unique primary structure, low specificity D-threonine aldolase from Arthrobacter sp. Strain DK-38. Molecular cloning and cofactor characterization [1].
• The gene encoding low specificity D-threonine aldolase, catalyzing the interconversion of D-threonine/D-allo-threonine and glycine plus acetaldehyde, was cloned from the chromosomal DNA of Arthrobacter sp. strain DK-38 [1].
• The introduction of a methyl side chain into G281 enhanced catalytic efficiency with the substrates D-threonine, D-allo-threonine, and L-serine, whereas the methyl side chain at position 279 impaired catalysis of all substrates as well as cofactor affinity [6].
• This finding suggests that glutamine catabolism may, like D-threonine, D-lysine, and glycine, bypass the positive activation of GDH and GAT controls [7].
• Other amino acids, including D-threonine, L-serine, and L-allo-threonine, were not effective substrates, indicating that PvdD has a high degree of substrate specificity [8].

Chemical compound and disease context of NSC 46702

• We have found that Pseudomonas putida ATCC 17642 cells grown in a medium containing D-threonine as the sole nitrogen source produce an enzyme that catalyzes epimerization of threonine [9].
• Isolation and characterization of D-threonine aldolase, a pyridoxal-5'-phosphate-dependent enzyme from Arthrobacter sp. DK-38 [10].
• The predicted amino acid sequence displayed 54% identity with that of D-threonine aldolase from gram-positive bacteria Arthrobacter sp. DK-38, but showed no significant similarity with those of other known pyridoxal-P enzymes [5].
• Conversion of DL-threonine, D-threonine and 2-oxobutyrate into propionate and 2-hydroxybutyrate by Fusobacterium species [11].

Biological context of NSC 46702

• These analyses indicate that the positive allosteric effector valine acts solely to alter the binding of D-threonine to the active sites of threonine deaminase by shifting the equilibrium between a low-affinity and high-affinity state, consistent with predictions from a simple two-state model [12].
• Nucleotide sequence, cloning, and overexpression of the D-threonine dehydrogenase gene from Pseudomonas cruciviae [13].

Anatomical context of NSC 46702

• Inhibition of growth and cell wall synthesis of Mycobacterium smegmatis by d-threonine [14].

Associations of NSC 46702 with other chemical compounds

• The increase in GS level could also be provoked by addition of D-lysine, D-threonine, or glycine to cells growing in an ammonia-rich medium [15].

Gene context of NSC 46702

• The rate of association of D-threonine with threonine deaminase in the presence of the regulatory ligands was biphasic [12].

References