The defect of TPP Ⅰ causes a disease, late infantile neuronal ceroid lipofuscinosis(LINCL, CLN2). To investigate the bio-activity of tripeptidyl peptidase Ⅰ(TPP Ⅰ) from rat kidneys, the effects of digestion of angiotensin Ⅱ(Ang Ⅱ) and a synthetic endo-type substrate(Gly 1 -Lys-Pro-...
TPP1 Antibody is a Rabbit Polyclonal antibody against TPP1. This gene encodes a member of the sedolisin family of serine proteases. The protease functions in the lysosome to cleave N-terminal tripeptides from substrates, and has weaker endopeptidase activity. It is synthesized as a catalytically-...
A gene on chromosome 11p15 that encodes a sedolisin-type serine protease, which acts in lysosomes to cleave N-terminal tripeptides from substrates; it also has weak endopeptidase activity. Tripeptidyl peptidase I is activated and auto-proteolysed by acidification.Molecular pathologyTPP1 mutations have...
The activity is increased by stress, such as during starvation and muscle wasting, and in tumour cells. Overexpression of TPP II leads to accelerated cell growth, genetic instability and resistance to apoptosis, whereas inhibition or down-regulation of TPP II renders cells sensitive to apoptosis. ...
In addition to exopeptidase activity, Quaternary structure of TPPII The first electron micrographs of negatively stained TPPII particles isolated from human erythrocytes were already published in 1996 and showed that the subunits assemble into a large oligomeric structure [53]. Also Drosophila TPPII (...
The enzyme had a maximal activity at pH 3.0 for an endopeptidase substrate, but at pH 4.5 with respect to tripeptidyl peptidase activity. Both endopeptidase and tripeptidyl peptidase activities were strongly inhibited by Ala-Ala-Phe-CH2Cl, but not inhibited by tyrostatin, an inhibitor of ...
The secreted proteolytic activity of Aspergillus fumigatus is of potential importance as a virulence factor and in the industrial hydrolysis of protein sources. The A. fumigatus genome contains sequences that could encode a five-member gene family that produces proteases in the sedolisin family (MEROPS...
Due to its aminopeptidase activity, TPPII was sug- gested to function as a post-proteasomal trimpeptidase for epitope pre- cursor molecules20. In addition to its exo-peptidase activity, TPPII also exhibits endo-proteolytic cleavage properties and it is able to cleave after lysine residues19. ...
However, Pro or Lys in the P 1 position and Pro in the P 1′ positions are incompatible with TPP-I activity. These observations suggest that TPP-I is a non-specific, but essential, peptidase involved in the latter stages of lysosomal protein degradation. 展开 关键词:...
Human tripeptidyl-peptidase I (TPP I, CLN2 protein) is a lysosomal serine protease that removes tripeptides from the free N termini of small polypeptides and also shows a minor endoprotease activity. Due to various naturally occurring mutations, an inherited deficiency of TPP I activity causes ...