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

BRENDA support

Literature summary for 3.4.24.64 extracted from

  • Geli, V.
    Functional reconstitution in Escherichia coli of the yeast mitochondrial matrix peptidase from its two inactive subunits (1993), Proc. Natl. Acad. Sci. USA, 90, 6247-6251.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.64

Cloned(Commentary)

Cloned (Comment) Organism
coexpression of both subunits results in functionally active enzyme Saccharomyces cerevisiae
expressed in Escherichia coli Saccharomyces cerevisiae
Saccharomyces cerevisiae Saccharomyces cerevisiae

Localization

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
 overproducing strain VGA
-
Saccharomyces cerevisiae
-
 overproducing strains G10 (MAS1)
-

Purification (Commentary)

Purification (Comment) Organism
recombinant alpha- and beta-subunit separatly and as holoenzyme from Escherichia coli lysate Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Mitochondrial proteins with artificial precursors + H2O containing presequence of ATPase subunit 9 fused to dehydrofolate reductase, i.e. pre-Su9-DHFR Saccharomyces cerevisiae ?
-
 ?
additional information alpha-MPP (formerly MAS2) alone has no catalytic activity Saccharomyces cerevisiae ?
-
 ?

Subunits

Subunits Comment Organism
More alpha-MPP (formerly MAS2) alone has no catalytic activity Saccharomyces cerevisiae