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

BRENDA support

Literature summary for 3.4.24.B19 extracted from

  • Dunn, C.D.; Tamura, Y.; Sesaki, H.; Jensen, R.E.
    Mgr3p and Mgr1p are adaptors for the mitochondrial i-AAA protease complex (2008), Mol. Biol. Cell, 19, 5387-5397.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
Mgr1p Mgr3p and Mgr1p can bind substrate even in the absence of Yme1p, and both proteins are needed for maximal binding of an unfolded substrate by the i-AAA complex. Mgr3p and Mgr1p function together in an adaptor complex that seems to help target substrates to the i-AAA protease for degradation Saccharomyces cerevisiae
Mgr3p Mgr3p and Mgr1p can bind substrate even in the absence of Yme1p, and both proteins are needed for maximal binding of an unfolded substrate by the i-AAA complex. Mgr3p and Mgr1p function together in an adaptor complex that seems to help target substrates to the i-AAA protease for degradation Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial inner membrane
-
Saccharomyces cerevisiae 5743
-

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P32795
-
-

Synonyms

Synonyms Comment Organism
i-AAA Protease
-
Saccharomyces cerevisiae