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Literature summary for 3.2.1.45 extracted from

  • Sawkar, A.R.; Adamski-Werner, S.L.; Cheng, W.C.; Wonf, C.H.; Beutler, E.; Zimmer, K.P.; Kelly, J.W.
    Gaucher disease-associated glucocerebrosidases show mutation-dependent chenical chaperoning profiles (2005), Chem. Biol., 12, 1235-1244.
    View publication on PubMed

General Stability

General Stability Organism
chemical chaperones stabilize Gaucher disease-associated glucocerebroside variants N370S and G202R against misfolding, enabling their trafficking from the endoplasmic reticulum. The L44P variant is not chaperoned, likely because this mutation destabilizes a domain distinct from the catalytic domain Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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Gaucher disease-associated glucocerebroside variants N370S and G202R
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