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

BRENDA support

Literature summary for 3.4.21.88 extracted from

  • Kuhner, F.; Costa, L.T.; Bisch, P.M.; Thalhammer, S.; Heckl, W.M.; Gaub, H.E.
    LexA-DNA bond strength by single molecule force spectroscopy (2004), Biophys. J., 87, 2683-2690.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli interaction of enzyme with DNA motifs recA and yebG. Dissociation rate is 0.045 per s for recA and 0.13 per s for yebG with short-ranged binding potentials showing a stiff hydrogen-bonding network between protein and DNA ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information interaction of enzyme with DNA motifs recA and yebG. Dissociation rate is 0.045 per s for recA and 0.13 per s for yebG with short-ranged binding potentials showing a stiff hydrogen-bonding network between protein and DNA Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
More interaction of enzyme with DNA motifs recA and yebG. Dissociation rate is 0.045 per s for recA and 0.13 per s for yebG with short-ranged binding potentials showing a stiff hydrogen-bonding network between protein and DNA Escherichia coli