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Literature summary for 3.4.24.18 extracted from
- Protease domain glycans affect oligomerization, disulfide bond formation, and stability of the meprin A metalloprotease homooligomer (2006), J. Biol. Chem., 281, 37404-37415.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| N152Q/N270Q | no formation of intersubunit disulfide bonds and noncovalent association of subunits, loss of enzymatic activity | Mus musculus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mus musculus | - |
expression in HEK-293 cell | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | nine out of ten potential glycoslytation sites are glycosylated. Removal of two glycans at N234 and N270, as well as removal of glycan at N452, decrease the chemical and thermal stability of the homooligomer without affecting quarternary structure | Mus musculus |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | enzyme forms oligomers of ten or more subunits with intersubunit disulfide bonds and further association of subunits. No single glycan is essential for oligomer formation | Mus musculus |
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Release 2023.1 (January 2023)
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