Studies on Aspartase. II. On the Chemical Nature of Aspartase.

Metabolism of Aspartate by Propionibacterium freudenreichii subsp. shermanii : Effect on Lactate Fermentation

“…Aspartase was identified in propionibacteria in 1932 (27) and was later partially purified and characterized from Propionibacterium peterssonii (8,9). The metabolism by propionibacteria of amino acids, including aspartate, has been studied (3,23).…”

L ‐Aspartase: New Tricks from an Old Enzyme

“…Very early work (Cook and Woolf, 1928) detected aspartase activity in several different facultative aerobes. The initial definitive work on aspartase was a series of papers published from 1953 to 1954 by Ellfolk that reported the partial purification of the enzyme (Ellfolk, 1953a), metal ion and chemical modification studies (Ellfolk, 1953b), and an examination of the substrate specificity of aspartase (Ellfolk, 1954). Aspartase was initially purified by alcohol extraction, followed by either ammonium sulfate or acetone fractionation (Ellfolk, 1953a).…”

“…Aspartase has no activity with either D-aspartic acid or crotonic acid (Virtanen and Ellfolk, 1955), and earlier work showed that glycine, alanine, glutamine, maleic acid, and glutaconic acid were not substrates (Quastel and Woolf, 1926). Also, L-cysteic acid, diaminosuccinic acid, leucine, mesaconic acid, aconitic acid, sorbic acid, and the diamine or mono-or diethyl esters of fumaric acid have all failed to show turnover with this highly specific enzyme (Virtanen and Tarnanen, 1932;Ellfolk, 1954). While the specificity for L-aspartic acid had been clearly demonstrated, hydroxylamine was later found to be an alternative 3 00 VIOLA substrate for ammonia leading to the production of N-hydroxyaspartic acid (Emery, 1963).…”

Amino acid composition of soil organic matter and nitrogen transformations in soils under different management systems

“…Mg, is essential. Ellfolk (1953), however, reported negligible inhibition by fluoride, which is a known inhibitor of Ca-and Mg-containing enzymes. Several salts selected to provide a variety of cations and anions showed that soil aspartase activity was not inhibited when the TEIAM buffer used was prepared to contain 5 vnM with resjpect to the 92 following ions and compounds: K^ Na^ Ca®% Mg^% NOj", P04^, F, CI", S04^, NH/, fumaric acid, malic acid, and EDTA (Table 15).…”

“…Studies by Ellfolk (1953) on the chemistry of aspartase purified from Propionibacterium peterssonii showed that citrate, oxalate, ethylenediamine tetraacetic acid (EDTA), and pyrophosphate were strong inhibitors of this enzyme. The inhibition by cyanide, azide, and acetonitrile was weak, and no inhibition was observed by orthophosphate and sodium sulfide.…”