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Literature summary for 3.4.25.2 extracted from

  • Nishii, W.; Takahashi, K.
    Determination of the cleavage sites in SulA, a cell division inhibitor, by the ATP-dependent HslVU protease from Escherichia coli (2003), FEBS Lett., 553, 351-354.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
phenylmethylsulfonyl fluoride
-
Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
SulA + H2O Escherichia coli
-
additional information the enzyme produces 58 peptides with various sizes, 3-31 residues ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
SulA + H2O
-
Escherichia coli additional information the enzyme produces 58 peptides with various sizes, 3-31 residues ?
SulA + H2O the central and the C-terminal regions are preferentially cleaved. Major cleavage sites: Ala80-Ser81, Ala150-Ser151, Leu54-Gln55, Ile163-His164, Leu67-Thr68, Leu49-Leu50, Leu65-Trp66. No cleavage in absence of ATP Escherichia coli additional information the enzyme produces 58 peptides with various sizes, 3-31 residues ?

Cofactor

Cofactor Comment Organism Structure
ATP no cleavage of SulA in absence of ATP Escherichia coli