Literature summary for 4.1.1.65 extracted from

Ogunbona, O.; Onguka, O.; Calzada, E.; Claypool, S.
Multitiered and cooperative surveillance of mitochondrial phosphatidylserine decarboxylase 1 (2017), Mol. Cell. Biol., 37, e00049 .

Search for more literature for 4.1.1.65

Protein Variants

Protein Variants	Comment	Organism
K356/RF397L/E429G/M448T	mutations in beta-subunit. Mutant is temperature sensitive and autocatalytically impaired. Inner membrane proteases, Oma1p and Yme1p are responsible for degradation of the mutant precursor. Upon heat exposure postautocatalysis, mutant subunits accumulate in protein aggregates that are resolved by Yme1p acting alone, while the released alpha subunit is degraded in parallel by an unidentified protease	Saccharomyces cerevisiae

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	-	Saccharomyces cerevisiae	5739	-

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P39006	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	autocatalytic processing, precursor acts as self-processing serine protease	Saccharomyces cerevisiae

General Information

General Information	Comment	Organism
metabolism	the stability of endogenous Psd1 is influenced by inner membrane protease Yme1	Saccharomyces cerevisiae

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)