Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.21.53 extracted from

  • Rasulova, F.S.; Dergousova, N.I.; Starkova, N.N.; Melnikov, E.E.; Rumsh, L.D.; Ginodman, L.M.; Rotanova, T.V.
    The isolated proteolytic domain of Escherichia coli ATP-dependent protease Lon exhibits the peptidase activity (1998), FEBS Lett., 432, 179-181.
    View publication on PubMed
Search for more literature for 3.4.21.53

Cloned(Commentary)

Cloned (Comment) Organism
cloning the lon gene in pGEX-KG Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
25000
-
 LonP, gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli MH-1
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
casein + H2O
-
 Escherichia coli ?
-
 ?
casein + H2O
-
 Escherichia coli MH-1 ?
-
 ?
Melittin + H2O isolated proteolytic domain exhibits almost no activity toward casein, but hydrolyzes peptide substrates Escherichia coli ?
-
 ?
Melittin + H2O isolated proteolytic domain exhibits almost no activity toward casein, but hydrolyzes peptide substrates Escherichia coli MH-1 ?
-
 ?
additional information isolated proteolytic domain exhibits the peptidase activity Escherichia coli ?
-
 ?
additional information isolated proteolytic domain exhibits the peptidase activity Escherichia coli MH-1 ?
-
 ?

Synonyms

Synonyms Comment Organism
protease lon
-
 Escherichia coli