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Literature summary extracted from

  • Tschantz, W.R.; Paetzel, M.; Cao, G.; Suciu, D.; Inouye, M.; Dalbey, R.E.
    Characterization of a soluble, catalytically active form of Escherichia coli leader peptidase: requirement of detergent or phospholipid for optimal activity (1995), Biochemistry, 34, 3935-3941.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.21.89 Phospholipids stimulate Escherichia coli
3.4.21.89 Triton X-100 stimulates activity with pro-OmpA-nuclease A or a peptide substrate Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.21.89 0.032
-
 pro-OmpA-nuclease A
-
 Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.89 membrane the catalytic domain extends into the periplasmic space and is anchored to the membrane by two transmembrane segments located at the N-terminal end of the protein Escherichia coli 16020
-

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.89 Escherichia coli
-
 soluble form of the leader peptidase DELTA2-75
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.89 Hybrid protein pro-OmpA-nuclease A + H2O
-
 Escherichia coli ?
-
 ?
3.4.21.89 pro-OmpA-nuclease A + H2O
-
 Escherichia coli OmpA-nuclease A + ?
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.21.89 3
-
 pro-OmpA-nuclease A
-
 Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.89 additional information
-
 5.6 Escherichia coli