Tripeptidyl-peptidase I is apparently the CLN2 protein absent in classical late-infantile neuronal ceroid lipofuscinosis

Biochim Biophys Acta. 1999 Jan 11;1429(2):496-500. doi: 10.1016/s0167-4838(98)00238-6.

Abstract

We report that fragments of amino acid sequence recently described for tripeptidyl-peptidase I (TPP I) show that it is the rat homologue of the human CLN2 gene product that is deficient in classical late-infantile neuronal ceroid lipofuscinosis. This is unexpected, since the CLN2 protein has been thought to be a carboxyl-dependent endopeptidase, but TPP I is an exopeptidase possibly of serine-type.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Aminopeptidases
  • Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
  • Endopeptidases / analysis*
  • Humans
  • Molecular Sequence Data
  • Neuronal Ceroid-Lipofuscinoses / enzymology*
  • Peptide Fragments / analysis
  • Peptide Hydrolases / analysis*
  • Sequence Alignment
  • Serine Proteases

Substances

  • Peptide Fragments
  • Endopeptidases
  • Peptide Hydrolases
  • Serine Proteases
  • Aminopeptidases
  • Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
  • tripeptidyl-peptidase 1