Inhibition of aspartate β-decarboxylase by aminomalonate. Stereospecific decarboxylation of aminomalonate to glycine

Two Forms of Serine Transhydroxymethylase, One Absent in a Thymidylate‐less Mutant in Saccharomyces cerevisiae

“…Similar differences in stability, chromatography and electrophoretic mobility, were found [4,5] for the two isoenzymes, the mitochondrial and the cytoplasmic ones, purified from rat liver. Mechanistic and stereochemical studies showed that the cytoplasmic enzyme catalyses the aldol cleavage of allothreonine and the decarboxylation of aminomalonate as well as serine transhydroxymethylation, but the mitochondrial enzyme catalyses only the serine transhydroxymethylation [5].…”

“…Mechanistic and stereochemical studies showed that the cytoplasmic enzyme catalyses the aldol cleavage of allothreonine and the decarboxylation of aminomalonate as well as serine transhydroxymethylation, but the mitochondrial enzyme catalyses only the serine transhydroxymethylation [5]. However, both isoenzymes purified from rabbit liver, the cytoplasmic and the mitochondrial ones, exhibited similar ratios of serine transhydroxymethylase/threonine (allothreonine) aldolase activities [3].…”

Evidence for l-threonine cleavage and allothreonine formation by different enzymes from Clostridium pasteurianum: threonine aldolase and serine hydroxymethyltransferase

“…organism apparently does not attack any ofthe substrates (Bell & Turner, 1977). On the other hand, in rat liver cytoplasm an enzyme with specificity similar to that of the clostridial threonine aldolase has been detected (Palekar et al, 1973).…”

Enzymatically catalysed decarboxylation of β-carboxyaspartic acid (Asa)

“…The kinetics of thermal decarboxylation of the three synthetically prepared carboxy amino acids have been compared (8). Enzymes catalysing the decarboxylation of Ama have been described (9,10). W e wish to report the demonstration of Asa decarboxylase activity in an extract of E. coli.…”