A pyridoxal-phosphate protein. With one component of the animal enzyme, 2-oxobutanoate can replace glyoxylate. A second component also catalyses the reaction of EC 2.6.1.51 serine---pyruvate transaminase.
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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SYSTEMATIC NAME
IUBMB Comments
L-alanine:glyoxylate aminotransferase
A pyridoxal-phosphate protein. With one component of the animal enzyme, 2-oxobutanoate can replace glyoxylate. A second component also catalyses the reaction of EC 2.6.1.51 serine---pyruvate transaminase.
utilizes only glyoxylate as amino acceptor, hydroxypyruvate, 2-oxoglutarate, phenylpyruvate and 2-oxo-4-methyl-thiobutyrate are inactive, only L-alanine as amino donor, L-serine, L-threonine, L-glutamic acid, L-glutamine, L-aspartic acid, L-asparagine, L-ornithine, L-leucine, L-valine, L-isoleucine, L-histidine, L-phenylalanine, L-tryptophan and L-tyrosine are no substrates
enzyme knockout strain, 2% residual activity, no glycine auxotrophic phenotype. Glycine auxtrophy requires additional deletion of genes for threonine aldolase, and for mitochondrial and cytosolic serine hydroxymethyltransferase
enzyme knockout strain, 2% residual activity, no glycine auxotrophic phenotype. Glycine auxtrophy requires additional deletion of genes for threonine aldolase, and for mitochondrial and cytosolic serine hydroxymethyltransferase
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 25 mM-potassium phosphate buffer, pH 7.5, containing 100 mM NaCl, 0.1 mM pyridoxal 5'-phosphate and 10% glycerol, my be stored for at least 3 months without loss of activity
Characteristics of alanine: glyoxylate aminotransferase from Saccharomyces cerevisiae, a regulatory enzyme in the glyoxylate pathway of glycine and serine biosynthesis from tricarboxylic acid-cycle intermediates