Description
L-asparaginase catalyses the conversion of L-asparagine to L-aspartate. Two related families of asparaginase (L-asparagine amidohydrolase, EC:3.5.1.1) are designated type I and type II according to the terminology in Escherichia coli, which has both: L-asparaginase I is a low-affinity enzyme found in the cytoplasm, while L-asparaginase II is a high-affinity periplasmic enzyme synthesized with a cleavable signal sequence. This family describes L-asparaginases related to type II of E. coli. Both the cytoplasmic and the cell wall asparaginases of Saccharomyces cerevisiae belong to this set. Members of this set from Acinetobacter glutaminasificans and Pseudomonas fluorescens are described as having both glutaminase and asparaginase activities [PMID: 10499283, PMID: 3379033]. All members are homotetrameric.