Tripeptidyl peptidase

spinqualitylabelsall models Glycosylated tripeptidyl peptidase I dimer complex with sulfate, Zn+2 (grey), Ca+2 (green) and Cl- (green) ions, 3ee6 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Tripeptidyl peptidase or tripeptidyl aminopeptidase (TPP) is an enzyme which cleaves N-terminal tripeptides from polypeptides. TPP-I functions in lysosomes. TPP-II is part of the ubiquitin-proteasome pathway. TPP-IV is a serine exopeptidase which cleaves proline dipeptides from the N-terminus of polypeptides. Didease TPP-I participates in lysosomal turnover of proteins in pathological conditions associated with cell injury and its mutations cause the fatal neurodegenerative childhood neuronal ceroid lipofuscinosis. TPP-II deficiency is linked to severe autoimmunity. TPP-II has central and peripheral roles in metabolism and hence in fat formation. Structural highlights TPP-I catalytic triad is the typical Ser-Glu-Asp and the active site contains an octahedrally coordinated Ca+2 ion.

3D Structures of Tripeptidyl peptidase

Updated on 17-May-2022

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• Tripeptidyl peptidase-I
  • 3ee6 – TPP-I – human
    
  • 3edy – hTPP-I precursor residues 20-563
    
• Tripeptidyl peptidase-II
  • 3lxu – TPP-II residues 463-770 – Drosophila melanogaster
    
• Tripeptidyl peptidase-IV
  • 2eep – PgPro-TPP-IV+inhibitor – Porphyromonas gingivalis
    
  • 2d5l - PgPro-TPP-IV
    
  • 2z3w - PgPro-TPP-IV (mutant)
    
  • 2z3z - PgPro-TPP-IV (mutant)+inhibitor
    
  • 2dcm - PgPro-TPP-IV (mutant) + substrate
    

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Alexander Berchansky, Michal Harel, Joel L. Sussman