Identification of the zinc binding ligands and the catalytic residue in human aspartoacylase, an enzyme involved in Canavan disease

@article{Herga2006IdentificationOT,
  title={Identification of the zinc binding ligands and the catalytic residue in human aspartoacylase, an enzyme involved in Canavan disease},
  author={S. Herga and J. Berrin and J. Perrier and A. Puigserver and T. Giardina},
  journal={FEBS Letters},
  year={2006},
  volume={580}
}
Canavan disease is an autosomal‐recessive neurodegenerative disorder caused by a lack of aspartoacylase, the enzyme that degrades N‐acetylaspartate (NAA) into acetate and aspartate. With a view to studying the mechanisms underlying the action of human aspartoacylase (hASP), this enzyme was expressed in a heterologous Escherichia coli system and characterized. The recombinant protein was found to have a molecular weight of 36 kDa and kinetic constants K m and k cat of 0.20 ± 0.03 mM and 14.22… Expand
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Publisher Summary This chapter covers the structural chemistry and the biological aspects of carboxypeptidase A (CPD A). Carboxypeptidase A gets its name from the fact that it prefers peptide andExpand
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TLDR
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