Skip NavigationSkip to Content
Return Return to Search Results

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

  1. Author:
    Prahl, A.
    Pazgier, M.
    Hejazi, M.
    Lockau, W.
    Lubkowski, J.

  2. Author Address

    Lubkowski, J, NCI, Macromol Crystallog Lab, Frederick, MD 21702 USA NCI, Macromol Crystallog Lab, Frederick, MD 21702 USA. Humboldt Univ, Inst Biol, D-10115 Berlin, Germany.
    1. Year: 2004
  2. Journal: Acta Crystallographica Section D-Biological Crystallography
    1. 60
    2. Part 6
    3. Pages: 1173-1176
  4. Type of Article: Article
  1. Abstract:

    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 Angstrom, 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 alpha-subunits and two beta-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 N-4-(beta-N-acetylglucosaminyl)-L-asparagine, the substrate of glycosylasparaginases

    See More

  1. Keywords:

External Sources

  1. No sources found.

Library Notes

  1. No notes added.
NCI at Frederick

You are leaving a government website.

This external link provides additional information that is consistent with the intended purpose of this site. The government cannot attest to the accuracy of a non-federal site.

Linking to a non-federal site does not constitute an endorsement by this institution or any of its employees of the sponsors or the information and products presented on the site. You will be subject to the destination site's privacy policy when you follow the link.

ContinueCancel