ENTRY       EC 3.4.99.36
NAME        Leader peptidase
            Signal peptidase I
CLASS       Hydrolases
            Acting on peptide bonds (peptidases)
            Endopeptidases of unknown catalytic mechanism
REACTION    Cleavage of N-terminal leader sequences from secreted proteins
SUBSTRATE   Protein
            H2O
PRODUCT     Protein
            Peptide
COMMENT     A 36 kDa enzyme in the inner and outer membranes of E. coli. Not
            inhibited by phenylmethylsulfonyl fluoride or 1,10-phenanthroline.
            Cleaves a single bond Ala+Ala in M13 phage procoat protein, so
            producing free leader (signal) peptide and coat protein. Also
            accurately cleaves a 16-residue synthetic peptide that spans the
            normal cleavage site. The characteristics of the P1 and P3
            residues are especially important in the specificity of leader
            peptidase.  Leader peptidases that may have somewhat
            different specificities are known eukaryotic organisms also.
DBLINKS     University of Geneva ENZYME DATA BANK: 3.4.99.36
            WIT (What Is There) Metabolic Reconstruction: 3.4.99.36
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