Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.19.12 extracted from

  • Nagamine, S.; Kabuta, T.; Furuta, A.; Yamamoto, K.; Takahashi, A.; Wada, K.
    Deficiency of ubiquitin carboxy-terminal hydrolase-L1 (UCH-L1) leads to vulnerability to lipid peroxidation (2010), Neurochem. Int., 57, 102-110.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
DTT required, hydrolase activity of UCH-L1 in vitro is decreased when reducing dithiothreitol is omitted from the reaction buffer Mus musculus
additional information UCH-L1 is easily affected by redox status Mus musculus

Protein Variants

Protein Variants Comment Organism
additional information deficiency of UCH-L1 of gad mice, i.e. UCH-L1-deficient mutant gracile axonal dystrophy mice, leads to vulnerability to lipid peroxidation both in vivo and in vitro. When neurons from dorsal root ganglions are cultured in the vitamin E-free medium, cell death is increased in the neurons of gad mice. Oxidative stress, especially lipid peroxidation, augments the neuronal cell death of gad mice Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
additional information UCH-L1 is easily affected by redox status Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol UCH-L1 itself is a soluble protein and has no transmembrane domain, but UCH-L1 directly and specifically binds to phosphatidic acid thereby interacting with the menbrane Mus musculus 5829
-
plasma membrane UCH-L1 itself is a soluble protein and has no transmembrane domain, but UCH-L1 directly and specifically binds to phosphatidic acid thereby interacting with the menbrane. Monoubiquitin can possibly regulate the interaction between UCH-L1 and phosphatidic acid since bound UCH-L1 is increased in the presence of monoubiquitin Mus musculus 5886
-

Organism

Organism UniProt Comment Textmining
Mus musculus
-
C57BL/6J mice
-
Mus musculus C57/BL6J
-
C57BL/6J mice
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information cysteine residues of UCH-L1 are readily carbonylated by 4-hydroxy-2-nonenal or other unsaturated aldehydes, and the carbonylated UCH-L1 exhibits altered properties in hydrolase activity and protein-protein interactions Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
neuron UCH-L1 is localized on the inside of the plasma membrane of dorsal root ganglion neurons Mus musculus
-

Synonyms

Synonyms Comment Organism
ubiquitin carboxy-terminal hydrolase-L1
-
Mus musculus
ubiquitin carboxyterminal hydrolase-L1
-
Mus musculus
UCH-L1
-
Mus musculus

General Information

General Information Comment Organism
malfunction deficiency of UCH-L1 leads to vulnerability to lipid peroxidation both in vivo and in vitro Mus musculus