This enzyme acts in concert with EC 2.3.1.29, glycine C-acetyltransferase, in the degradation of threonine to glycine. This threonine-degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex . In aqueous solution, the product L-2-amino-3-oxobutanoate can spontaneously decarboxylate to form aminoacetone.
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The taxonomic range for the selected organisms is: Mus musculus The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
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SYSTEMATIC NAME
IUBMB Comments
L-threonine:NAD+ oxidoreductase
This enzyme acts in concert with EC 2.3.1.29, glycine C-acetyltransferase, in the degradation of threonine to glycine. This threonine-degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex [2]. In aqueous solution, the product L-2-amino-3-oxobutanoate can spontaneously decarboxylate to form aminoacetone.
embryonic stem cells are critically dependent on the amino acid threonine, and threonine catabolism via the TDH enzyme is important to the growth and metabolic state of mouse embryonic stem cells
embryonic stem cells are critically dependent on the amino acid threonine, and threonine catabolism via the TDH enzyme is important to the growth and metabolic state of mouse embryonic stem cells
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo form, in complex with NAD+ and glycerol, or with only NAD+, sitting drop vapor diffusion method, using 0.1 M HEPES (pH 7.0), 10% (w/v) PEG 4000, 10% (v/v) 2-propanol, or 0.2 M NaCl, 0.1 M HEPES (pH 7.5), 25% (w/v) PEG3350