Mammalian pitrilysin: substrate specificity and mitochondrial targeting.

ABSTRACT: The substrate specificity of the mitochondrial metallopeptidase proteinase 1 (MP1) was investigated and its mitochondrial targeting signal identified. The substrate specificity of MP1 was examined with physiological peptides as substrates. Although the enzyme exhibits broad substrate specificity, there is a trend for peptides containing 13 or more residues to exhibit K(m) values of 2 muM or less. Three of four peptides containing 11 or fewer residues exhibited K(m) values above 10 muM. Similarly, peptides containing 13 or more residues exhibited k(cat) values below 10 min(-1), while three of four peptides containing 11 or fewer residues exhibited k(cat) values above 30 min(-1). Many of the peptide cleavage sites of MP1 resemble that of the mitochondrial processing protease (MPP); however,

SUBMITTER: Chow KM 

PROVIDER: S-EPMC2765508 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature