Literature summary for 3.2.1.23 extracted from

Vera, A.; Aris, A.; Daura, X.; Martinez, M.A.; Villaverde, A.
Engineering the E. coli beta-galactosidase for the screening of antiviral protease inhibitors (2005), Biochem. Biophys. Res. Commun., 329, 453-456.

Search for more literature for 3.2.1.23

Protein Variants

Protein Variants	Comment	Organism
additional information	engineering the Escherichia coli beta-galactosidase for the screening of antiviral protease inhibitors. Identification of a new accomodation site between amino acids 581 and 582, in a solvent-exposed and flexible beta-turn of domain III. the replacement of the model peptide reproducing the matrix-capsid (p17/p24) gag cleavage sequence renders a highly active and efficiently digested chimeric construct. The use of this insertion site, that increases the cleavage potential of this reporter enzyme, can improve the sensitivity and dynamic range of the antiviral drug assay	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P00722	-	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)