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Literature summary for 3.4.24.70 extracted from

  • Novak, P.; Dev, I.K.
    Degradation of a signal peptide by protease IV and oligopeptidase A (1988), J. Bacteriol., 170, 5067-5075.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.70

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
 Escherichia coli 5737
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Prolipoprotein signal peptide + H2O Escherichia coli further degrades partially degraded portions of signal peptide yielded by protease IV ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
to near homogeneity Escherichia coli

Storage Stability

Storage Stability Organism
4°C, in 0.25 M potassium phosphate buffer, pH 8, at least 6 months Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information substrates are N-blocked peptides with at least 4 amino acid residues or unblocked pentapeptides, no substrates are signal peptide still attached to the mature protein Escherichia coli ?
-
 ?
Prolipoprotein signal peptide + H2O proposed cleavage sites Escherichia coli Hydrolyzed prolipoprotein signal peptide peptide fragments identified ?
Prolipoprotein signal peptide + H2O methionine-labelled Escherichia coli Hydrolyzed prolipoprotein signal peptide peptide fragments identified ?
Prolipoprotein signal peptide + H2O further degrades partially degraded portions of signal peptide yielded by protease IV Escherichia coli ?
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli