Ribonucleotide Reductase Protein R1; domain 1
Studies on aspartase. II. Role of sulfhydryl groups in aspartase from Escherichia coli.
Studies on aspartase. V. Denaturant-mediated reactivation of aspartase, which has been otherwise irreversibly inactivated by various causes.
Acetylation-induced alteration of catalytic and regulatory properties of aspartase.
L-aspartase from Escherichia coli: substrate specificity and role of divalent metal ions.
Effect of detergents on aspartate ammonia-lyase activity in Escherichia alcalescens.
Activation of aspartase by site-directed mutagenesis.
Use of hybridization for distance measurement by fluorescence energy transfer in oligomeric proteins: distance between two functional sites in aspartase.
Cloning and nucleotide sequence of the Bacillus subtilis ansR gene, which encodes a repressor of the ans operon coding for L-asparaginase and L-aspartase.
Characterization of three types of aspartase activated by site-directed mutagenesis, limited proteolysis, and acetylation.
Crystallization and preliminary X-ray studies of L-aspartase from Escherichia coli.
Elimination of the sensitivity of L-aspartase to active-site-directed inactivation without alteration of catalytic activity.
The multisubunit active site of fumarase C from Escherichia coli.
The structure of L-aspartate ammonia-lyase from Escherichia coli.
Evaluation of functionally important amino acids in L-aspartate ammonia-lyase from Escherichia coli.
Studies on the properties of mutants of aspartase from Escherichia coli W.
Recovery of catalytic activity from an inactive aggregated mutant of l-aspartase.
L-aspartase: new tricks from an old enzyme.
Cloning and over-expression of thermostable Bacillus sp. YM55-1 aspartase and site-directed mutagenesis for probing a catalytic residue.
A monomeric L-aspartase obtained by in vitro selection.
Although this enzyme requires a divalent metal ion per subunit, it is not involved in catalytic reaction, according to the literature [4]. It may contribute to the stability of the enzyme (see [17]).