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Literature summary for 3.4.24.64 extracted from

  • Mukhopadhyay, A.; Yang, C.S.; Wei, B.; Weiner, H.
    Precursor protein is readily degraded in mitochondrial matrix space if the leader is not processed by mitochondrial processing peptidase (2007), J. Biol. Chem., 282, 37266-37275.
    View publication on PubMed
Search for more literature for 3.4.24.64

Protein Variants

Protein Variants Comment Organism
additional information yeast aldehyde dehydrogenase and malate dehydrogenase are mutated so that they would not be processed by the enzyme after import into the mitochondrial matrix space, the mutant nonprocessed enzymes are functional but instable, the nonprocessed precursors are degraded in the matrix space, expression in HWTHL10 cells, overview Saccharomyces cerevisiae
additional information yeast malate dehydrogenase and human, yeast, or rat liver aldehyde dehydrogenases are mutated so that they would not be processed by the enzyme after import into the mitochondrial matrix space, the mutant nonprocessed enzymes are functional but instable, the nonprocessed precursors are degraded in the matrix space, expression in HeLa cells, overview Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
o-phenanthroline enzyme inhibition leads to degradation of the unprocessed preproteins in the mitochondrial matrix space Homo sapiens
o-phenanthroline enzyme inhibition leads to degradation of the unprocessed preproteins in the mitochondrial matrix space Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion mitochondrial matrix space Homo sapiens 5739
-
mitochondrion mitochondrial matrix space Saccharomyces cerevisiae 5739
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens the mitochondrial processing peptidase removes leader peptides of preproteins after import into the mitochondrial matrix space to increase protein stability, enzyme inhibition leads to degradation of the unprocessed preproteins in the mitochondrial matrix space, overview ?
-
 ?
additional information Saccharomyces cerevisiae the mitochondrial processing peptidase removes leader peptides of preproteins after import into the mitochondrial matrix space to increase protein stability, enzyme inhibition leads to degradation of the unprocessed preproteins in the mitochondrial matrix space, overview ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Saccharomyces cerevisiae
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
HeLa cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the mitochondrial processing peptidase removes leader peptides of preproteins after import into the mitochondrial matrix space to increase protein stability, enzyme inhibition leads to degradation of the unprocessed preproteins in the mitochondrial matrix space, overview Homo sapiens ?
-
 ?
additional information the mitochondrial processing peptidase removes leader peptides of preproteins after import into the mitochondrial matrix space to increase protein stability, enzyme inhibition leads to degradation of the unprocessed preproteins in the mitochondrial matrix space, overview Saccharomyces cerevisiae ?
-
 ?

Synonyms

Synonyms Comment Organism
MPP
-
 Homo sapiens
MPP
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
27
-
 assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
 assay at Saccharomyces cerevisiae