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Literature summary for 3.4.24.64 extracted from

  • Osman, C.; Wilmes, C.; Tatsuta, T.; Langer, T.
    Prohibitins interact genetically with Atp23, a novel processing peptidase and chaperone for the F1Fo-ATP synthase (2007), Mol. Biol. Cell, 18, 627-635.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.64

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type enzyme and enzyme mutants in DELTA atp23cells Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
E168Q site-directed mutation in the consensus metal-binding site, the active site residue mutant is proteolytically inactive, but shows processing of the Atp6 subunit of pre-F1FO-ATP synthase Saccharomyces cerevisiae
H167A site-directed mutation in the consensus metal-binding site, the mutant does not show processing of the Atp6 subunit of pre-F1FO-ATP synthase Saccharomyces cerevisiae
H171A site-directed mutation in the consensus metal-binding site, the mutant does not show processing of the Atp6 subunit of pre-F1FO-ATP synthase Saccharomyces cerevisiae
additional information deletion of ATP23 completely inhibits the assembly of the mitochondrial-encoded FO-subunits into the F1FO-ATP synthase, which is observed in wild-type mitochondria Saccharomyces cerevisiae

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
additional information consensus metal-binding motif HEliH, formed by amino acid residues 167-171 of Atp23 Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Saccharomyces cerevisiae the enzyme genetically interacts with prohibitins in the inner mitochondrial membrane and links the function of prohibitins to the F1FO-ATP synthase complex ?
-
 ?
pre-F1FO-ATP synthase + H2O Saccharomyces cerevisiae on one hand, Atp23 serves as a processing peptidase and mediates the maturation of the mitochondrially-encoded FO-subunit Atp6 after its insertion into the inner membrane, on the other hand, independent of its proteolytic activity, Atp23 promotes the association of mature Atp6 with Atp9 oligomers with chaperone activity, overview, the assembly step is thus under the control of two substrate-specific chaperones, Atp10 and Atp23, which act on opposite sides of the inner membrane, modelling of assembly, overview mature F1FO-ATP synthase + prepeptide
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
 wild-type strain S288c and derivatives
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme genetically interacts with prohibitins in the inner mitochondrial membrane and links the function of prohibitins to the F1FO-ATP synthase complex Saccharomyces cerevisiae ?
-
 ?
pre-F1FO-ATP synthase + H2O on one hand, Atp23 serves as a processing peptidase and mediates the maturation of the mitochondrially-encoded FO-subunit Atp6 after its insertion into the inner membrane, on the other hand, independent of its proteolytic activity, Atp23 promotes the association of mature Atp6 with Atp9 oligomers with chaperone activity, overview, the assembly step is thus under the control of two substrate-specific chaperones, Atp10 and Atp23, which act on opposite sides of the inner membrane, modelling of assembly, overview Saccharomyces cerevisiae mature F1FO-ATP synthase + prepeptide
-
 ?
pre-F1FO-ATP synthase + H2O putative catalytically active Glu168 Saccharomyces cerevisiae mature F1FO-ATP synthase + prepeptide
-
 ?

Synonyms

Synonyms Comment Organism
Atp23
-
 Saccharomyces cerevisiae
processing peptidase
-
 Saccharomyces cerevisiae