3.4.24.59: mitochondrial intermediate peptidase
This is an abbreviated version!
For detailed information about mitochondrial intermediate peptidase, go to the full flat file.
Word Map on EC 3.4.24.59
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3.4.24.59
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mpp
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presequence
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oct1
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mating-type
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tetrapolarity
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schizophyllum
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homobasidiomycetes
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heterothallic
- 3.4.24.59
- mpp
- presequence
- oct1
-
mating-type
-
tetrapolarity
-
schizophyllum
- homobasidiomycetes
-
heterothallic
Reaction
release of an N-terminal octapeptide as second stage of processing of some proteins imported into the mitochondrion =
Synonyms
At1g09300, hMIP, Icp55, MIP, MIP1, MIPEP, mitochondrial intermediate peptidase, OCT1, octapeptidyl aminopeptidase 1, Proteinase, mitochondrial intermediate precursor-processing
ECTree
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General Information
General Information on EC 3.4.24.59 - mitochondrial intermediate peptidase
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malfunction
physiological function
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cleavage of Notch recptor at the S5 site is abolished in MIEP knockout cells
malfunction
down-regulation of the putative Trypanosoma brucei mitochondrial intermediate peptidase (MIP) homolog by RNAi renders the cells unable to grow after 48 hours of induction. Ablation of MIP results in the accumulation of the precursor of the trypanosomatid-specific trCOIV protein, the largest nuclear-encoded subunit of the cytochrome c oxidase complex in this flagellate
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Notch function can be modulated by MIPEP-mediated cleavage. Results show that S5 site proteolysis represents a novel regulatory component of Notch signaling
physiological function
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the stability of intermediate and mature forms of Oct1 substrate proteins in organello and in vivo is compared. Oct1 cleavage increases the half-life of its substrate proteins, most likely by re-moving destabilizing amino acids at the intermediate's N-terminus. Oct1 converts unstable precursor intermediates generated by mitochondrial processing peptidase (MPP) into stable mature proteins. Oct1 acts as a quality control system for MPP-processed preproteins
physiological function
the enzyme plays a role in stabilizing mitochondrial proteins by the removal of single amino acids from mitochondrial processing peptidase-processed proteins