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Literature summary for 3.4.21.89 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

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

KM Value [mM]

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

Localization

Localization Comment Organism GeneOntology No. Textmining
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

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

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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

pH Optimum

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