Recombinant Human PPT1/PPT protein

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

PPT1 also known as palmitoyl-protein thioesterase 1 is an enzyme that plays a critical role in protein metabolism by removing thioester-linked palmitate groups from proteins. This enzyme has a molecular weight of approximately 37 kDa. PPT1 is expressed widely in the body with significant expression in tissues such as the brain and liver. It localizes primarily in the lysosomes where it assists in lysosomal degradation pathways. Polyclonal antibodies against PPT1 can be utilized in protein analysis and help elucidate the structure and functionality of this enzyme further.

Biological function summary

PPT1 contributes to the turnover and stability of proteins by mediating their de-palmitoylation an important step in maintaining appropriate protein function and cellular homeostasis. This enzyme assists in the recycling and degradation process by facilitating the catabolism of proteins through the lysosomal pathway. PPT1 does not function as part of a larger complex but operates individually to execute the removal of palmitate which impacts a diverse range of substrates vital for controlling cellular mechanisms such as synaptic function.

Pathways

PPT1 is heavily involved in the protein degradation pathway within lysosomes. This pathway is important for the autophagic degradation process which directly associates with cellular waste management and the recycling of cellular components. PPT1's function is also connected to protein stability because improper palmitoylation can disrupt protein location and function. The enzyme shows functional interaction with proteins like CLN2 which also participates in lysosomal degradation processes and they share involvement in neuronal homeostasis.

Associated diseases and disorders

Defects in PPT1 activity lead to neurodegenerative conditions notably the Infantile Neuronal Ceroid Lipofuscinosis (INCL). This disorder results from the accumulation of lipid-protein complexes in neurons emphasizing the need for proper PPT1 function. PPT1 has connections to the disease context through its interaction with the protein CLN3 another gene implicated in Batten disease part of the neuronal ceroid lipofuscinoses group. The study of PPT1 opens avenues for therapeutic approaches targeting these lysosomal storage disorders. Immunohistochemistry and immunocytochemistry are techniques often used to study the role of PPT1 in these pathological states.