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Structure of the isoaspartyl peptidase withl-­asparaginase activity from Escherichia coli

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Abstract:

The crystal structure of the Escherichia coli enzyme (EcAIII) with isoaspartyl dipeptidase andl-asparaginase activity has been solved and refined to a resolution of 1.65 Å, with crystallographic R-factor and Rfree values of 0.178 and 0.209, respectively. EcAIII belongs to the family of N-terminal hydrolases. The amino-acid sequence of EcAIII is homologous to those of putative asparaginases from plants. The structure of EcAIII is similar to the structures of glycosylasparaginases. The mature and catalytically active form of EcAIII is a heterotetramer consisting of two α-subunits and two -subunits. Both of the equivalent active sites present in the EcAIII tetramer is assisted by a metal-binding site. The metal cations, modelled here as Na+, have not previously been observed in glycosylasparaginases. This reported structure helps to explain the inability of EcAIII and other plant-type asparaginases to hydrolyze N4-(-N-acetylglucosaminyl)-l-asparagine, the substrate of glycosylasparaginases.

Keywords: E. coli enzymes; Na+ sites; isoaspartyl dipeptidases; plant-type asparaginases

Document Type: Short Communication

DOI: https://doi.org/10.1107/S0907444904003403

Publication date: 2004-06-01

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