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Literature summary for 3.4.23.49 extracted from

  • Neri, M.; Baaden, M.; Carnevale, V.; Anselmi, C.; Maritan, A.; Carloni, P.
    Microseconds dynamics simulations of the outer-membrane protease T (2008), Biophys. J., 94, 71-78.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
H212A molecular mechanics/coarse-grained (MM/CG) simulation applied Escherichia coli
S99A molecular mechanics/coarse-grained (MM/CG) simulation applied Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
outer membrane
-
 Escherichia coli 19867
-

Organism

Organism UniProt Comment Textmining
Escherichia coli P09169
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 structural and functional relationships for wild-type and mutated OmpT proteins investigated, relevant case of the Michaelis complex of the outer-membrane protease T (OmpT) analyzed by a hybrid molecular mechanics/coarse-grained (MM/CG) approach, structural explanation for decreased catalytic activity of the mutants S99A and H212A given Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-acetyl-Ala-Arg-Arg-Ala-methylamide + H2O fluctuations of outer-membrane protease OmpT in complex with its substrate Ala-Arg-Arg-Ala (ARRA) on microsecond timescale analyzed, effect of key point mutations at the active site studied Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
OmpT protein
-
 Escherichia coli
outer-membrane protease T
-
 Escherichia coli