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

BRENDA support

Literature summary for 1.1.1.34 extracted from

  • Lee, P.C.; Nguyen, A.D.; Debose-Boyd, R.A.
    Mutations within membrane domain of HMG CoA reductase confer resistance to sterol-accelerated degradation (2006), J. Lipid Res., 48, 318-327.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
A333P mutation disrupts Insig binding and abolishes sterol-accelerated degradation. The pivotal event for sterol-induced degradation of the choletsreol biosynthetic enzyme HMG-CoA reductase is binding of its membrane domain to Insig proteins in the endoplasmic reticulum. Insig are carriers for gp78, an E3 ubiquitin ligase that marks reductase for proteasomal degradation Cricetulus griseus
G87R mutation disrupts Insig binding and abolishes sterol-accelerated degradation. The pivotal event for sterol-induced degradation of the choletsreol biosynthetic enzyme HMG-CoA reductase is binding of its membrane domain to Insig proteins in the endoplasmic reticulum. Insig are carriers for gp78, an E3 ubiquitin ligase that marks reductase for proteasomal degradation Cricetulus griseus
S60N mutation disrupts Insig binding and abolishes sterol-accelerated degradation. The pivotal event for sterol-induced degradation of the choletsreol biosynthetic enzyme HMG-CoA reductase is binding of its membrane domain to Insig proteins in the endoplasmic reticulum. Insig are carriers for gp78, an E3 ubiquitin ligase that marks reductase for proteasomal degradation Cricetulus griseus

Organism

Organism UniProt Comment Textmining
Cricetulus griseus P00347
-
-

Source Tissue

Source Tissue Comment Organism Textmining
CHO-7 cell
-
Cricetulus griseus
-

Synonyms

Synonyms Comment Organism
HMG-CoA reductase
-
Cricetulus griseus