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Literature summary for 3.4.24.64 extracted from

  • Shimokata, K.; Kitada, S.; Ogishima, T.; Ito, A.
    Role of alpha-subunit of mitochondrial processing peptidase in substrate recognition (1998), J. Biol. Chem., 273, 25158-25163.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
cDNA of the precursor form of alpha and beta-MPP expressed in Escherichia coli BL21 Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
D378N constructed mutant Saccharomyces cerevisiae
D405N/D406N constructed mutant Saccharomyces cerevisiae
E197Q/E201Q constructed mutant Saccharomyces cerevisiae
E351Q constructed mutant Saccharomyces cerevisiae
E351Q/D352N/E353Q constructed mutant Saccharomyces cerevisiae
E353Q constructed mutant Saccharomyces cerevisiae
E377Q constructed mutant Saccharomyces cerevisiae
E377Q/D378N constructed mutant Saccharomyces cerevisiae
E395D constructed mutant Saccharomyces cerevisiae
H18A constructed mutant Saccharomyces cerevisiae
R8A constructed mutant Saccharomyces cerevisiae

Localization

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
yeast
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
adrenodoxin precursor + H2O processing Saccharomyces cerevisiae ?
-
?
aspartate aminotransferase + H2O processing Saccharomyces cerevisiae ?
-
?
malate dehydrogenase + H2O processing Saccharomyces cerevisiae ?
-
?

Subunits

Subunits Comment Organism
heterodimer consists of a alpha-mitochondrial processing peptidase and beta-MPP Saccharomyces cerevisiae