| Post Translational Modifications | A disulfide bond locks the enzyme in the closed conformation preventing substrate entry into the catalytic chamber. |
| Function | Metalloendopeptidase of the mitochondrial matrix that functions in peptide cleavage and degradation rather than in protein processing. Has an ATP-independent activity. Specifically cleaves peptides in the range of 5 to 65 residues. Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference. Degrades the transit peptides of mitochondrial proteins after their cleavage. Also degrades other unstructured peptides. It is also able to degrade amyloid-beta protein 40, one of the peptides produced by APP processing, when it accumulates in mitochondrion. It is a highly efficient protease, at least toward amyloid-beta protein 40. Cleaves that peptide at a specific position and is probably not processive, releasing digested peptides intermediates that can be further cleaved subsequently. It is also able to degrade amyloid-beta protein 42. |
| Protein Name | Presequence Protease - MitochondrialHprepPitrilysin Metalloproteinase 1Metalloprotease 1Hmp1 |
| Database Links | Reactome: R-HSA-1268020 |
| Cellular Localisation | MitochondrionMitochondrion Matrix |
| Alternative Protein Names | Presequence Protease - Mitochondrial proteinHprep proteinPitrilysin Metalloproteinase 1 proteinMetalloprotease 1 proteinHmp1 proteinPITRM1 proteinKIAA1104 proteinMP1 proteinPREP protein |
Information sourced from Uniprot.org
