Abstract
Three peptidases are responsible for the proteolytic processing of both nuclearly and mitochondrially encoded precursor polypeptides targeted to the various subcompartments of the mitochondria. Mitochondrial processing peptidase (MPP) cleaves the vast majority of mitochondrial proteins, while inner membrane peptidase (IMP) and mitochondrial intermediate peptidase (MIP) process specific subsets of precursor polypeptides. All three enzymes are structurally and functionally conserved across species, and their human homologues begin to be recognized as potential players in mitochondrial disease.
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, P.H.S.
-
Review
MeSH terms
-
Amino Acid Sequence
-
Animals
-
Binding Sites
-
Escherichia coli
-
Humans
-
Intracellular Membranes / enzymology*
-
Metalloendopeptidases / chemistry
-
Metalloendopeptidases / genetics
-
Metalloendopeptidases / metabolism*
-
Mitochondria / enzymology*
-
Mitochondrial Processing Peptidase
-
Mitochondrial Proteins / chemistry
-
Mitochondrial Proteins / metabolism
-
Molecular Sequence Data
-
Phylogeny
-
Protein Precursors / metabolism*
-
Saccharomyces cerevisiae
-
Sequence Alignment
-
Structure-Activity Relationship
-
Substrate Specificity
Substances
-
Mitochondrial Proteins
-
Protein Precursors
-
Metalloendopeptidases
-
mitochondrial intermediate peptidase