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Literature summary for 3.4.14.10 extracted from

  • Tomkinson, B.; Ni Laoi, B.; Wellington, K.
    The insert within the catalytic domain of tripeptidyl-peptidase II is important for the formation of the active complex (2002), Eur. J. Biochem., 269, 1438-1443.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in 293-cells, enzyme forms active oligomers Mus musculus
overexpression in 293-cells, enzyme i mainly in a nonassociated, inactive state Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information the recombinant human TPP II and murine TPP II display different association/dissociation characteristics when overexpressed in human 293-cells. The human enzyme is mainly in a nonassociated, inactive state, whereas the murine enzyme forms active oligomers. The formation of the active complex is profoundly influenced by a single amino acid difference: Gly252 in mouse and Arg252 in human Mus musculus
additional information the recombinant human TPP II and murine TPP II display different association/dissociation characteristics when overexpressed in human 293-cells. The human enzyme is mainly in a nonassociated, inactive state, whereas the murine enzyme forms active oligomers. The formation of the active complex is profoundly influenced by a single amino acid difference: Gly252 in mouse and Arg252 in human Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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Mus musculus
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Subunits

Subunits Comment Organism
More compared with other subtilases, TPP II has a 200 amino-acid insertion between the catalytic Asp44 and His264 residues and is active as an oligomeric complex. The insert is important for the formation of the active high-molecular mass complex Mus musculus
More compared with other subtilases, TPP II has a 200 amino-acid insertion between the catalytic Asp44 and His264 residues and is active as an oligomeric complex. The insert is important for the formation of the active high-molecular mass complex Homo sapiens