Ubiquitin C-terminal hydrolase L1 is a very plentiful protein found in the brain. It is estimated to make up 1 to 5 percent of the total neuron protein. The mutation and anomalous functions of this enzyme have been linked to numerous neurological disorders. This protein plays a significant role in the repair of axons and neurons after injury by getting rid of any unusual proteins by the Ubiquitin-proteasomes pathway and autophagy.
Ubiquitin C-terminal hydrolase L1 is an essential element for neuronal development mechanisms. It has an inhibitory impact on complexes containing mTOR, hence regulating the degeneration and synthesis of protein.
The composition of this enzyme is significant and specific to cells and neurons of the diffuse neuroendocrine system and their neoplasms. The catalytic triad of this protein is made of a cysteine at the point of 90, an aspartate at 176 and a histidine at 161. This catalytic triad is all accountable for its hydrolase activity.
UCHL1 belongs to the peptidase C12 family. The protein has one of the most compound knot structures and a five-knot crossing created for protein. The knotted structure is said to enhance the protein's resistance to degeneration in the proteasome. This is also a good indication of neuroprotection or diagnostics.
Ubiquitin C-terminal hydrolase L1 has been identified to display interactions with a-synuclein, a protein linked in the pathology of Parkinson's disease. It has also been shown to have an interaction with constitute photomorphogenic homolog subunit (COP9).
Besides, this enzyme has most recently been identified to interact with parkin, the E3 ligase. Parkin has been found to bind and ubiquitinylate the Ubiquitin C-terminal hydrolase L1 to enhance the lysosomal degradation of the enzyme.