Structure of the isoaspartyl peptidase with L-asparaginase activity from Escherichia coli

Adam Prahl, Marzena Pazgier, Mahdi Hejazi, Wolfgang Lockau, Jacek Lubkowski*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


The crystal structure of the Escherichia coli enzyme (EcAIII) with isoaspartyl dipeptidase and L-asparaginase activity has been solved and refined to a resolution of 1.65 Å, with crystallographic R-factor and R free 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 βsubunits. 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-(β-N- acetylglucosaminyl)-L-asparagine, the substrate of glycosylasparaginases.

Original languageEnglish
Pages (from-to)1173-1176
Number of pages4
JournalActa Crystallographica Section D: Biological Crystallography
Issue number6
StatePublished - Jun 2004


Dive into the research topics of 'Structure of the isoaspartyl peptidase with L-asparaginase activity from Escherichia coli'. Together they form a unique fingerprint.

Cite this