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Literature summary for 3.4.25.2 extracted from

  • Yoo, S.J.; Shim, Y.K.; Seong, I.S.; Seol, J.H.; Kang, M.S.; Chung, C.H.
    Mutagenesis of two N-terminal Thr and five Ser residues in HslV, the proteolytic component of the ATP-dependent HslVU protease (1997), FEBS Lett., 412, 57-60.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
S103A 50% of the activity of the wild-type enzyme with benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin in presence of the ATPase component HslU Escherichia coli
S124A 3% of the activity of the wild-type enzyme with benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin in presence of the ATPase component HslU Escherichia coli
S143A 95% of the activity of the wild-type enzyme with benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin in presence of the ATPase component HslU Escherichia coli
S172A 1% of the activity of the wild-type enzyme with benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin in presence of the ATPase component HslU Escherichia coli
S5A 124% of the activity of the wild-type enzyme with benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin in presence of the ATPase component HslU Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A7B8
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin + H2O
-
Escherichia coli benzyloxycarbonyl-GGL + 7-amino-4-methylcoumarin
-
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