منابع مشابه
Production of L-asparaginase II by Escherichia coli.
l-Asparaginase II was synthesized at constant rates by Escherichia coli under anaerobic conditions. The enzyme was produced optimally by bacteria grown between pH 7 and 8 at 37 C. Although some enzyme was formed aerobically, between 100 and 1,000 times more asparaginase II was produced during anaerobic growth in media enriched with high concentrations of a variety of amino acids. Bacteria grown...
متن کاملCrystal packing of plant-type L-asparaginase from Escherichia coli.
Plant-type L-asparaginases hydrolyze the side-chain amide bond of L-asparagine or its beta-peptides. They belong to the N-terminal nucleophile (Ntn) hydrolases and are synthesized as inactive precursor molecules. Activation occurs via the autoproteolytic release of two subunits, alpha and beta, the latter of which carries the nucleophile at its N-terminus. Crystallographic studies of plant-type...
متن کاملProduction and optimization of L-asparaginase in Escherichia coli
-ASPARAGINASE (L-ASNase) has been widely used as a therapeutic agent in the treatment for various lymphoblastic leukemia diseases. This study aimed to isolate and purify local bacterial isolates that are capable of producing L-ASNase, so 150 bacterial isolates from the Nile River where isolated, purified and their ability to produce L-ASNase was assessed. Among these isolates, 32 bacterial isol...
متن کاملL-asparaginase II of Escherichia coli. Studies on the enzymatic mechanism of action.
The enzymatic mechanism of asparaginase action has been explored using the acyl acceptor, hydroxylamine. Asparaginase catalyzed the synthesis of the hydroxamate from asparagine and more slowly from aspartic acid. P-Aspartohydroxamate was also a substrate for asparaginase. These reactions have rates which are linearly dependent on the concentration of the enzyme and can therefore be used as conv...
متن کاملL-Asparaginase from escherichia coli B. Succinylation and subunit interactions.
Asparaginase from Esckerickio coli B has been modified with increasing amounts of [r4C]succinic anhydride. Enzyme activity is enhanced when 15 % and 25 % of the lysyl residues are succinylated. Up to 40% of the lysyl residues were succinylated without destroying enzyme activity and without causing dissociation of this oligomeric protein. More extensive succinylation causes dissociation into sub...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1971
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)62536-0