Improvement of catalytic properties of Escherichia coli penicillin G acylase immobilized on glyoxyl agarose by addition of a six-amino-acid tag.
A tag of three lysines alternating with three glycines was added to the C-terminal end of the beta chain of penicillin G acylase (PGA). This modification improved the immobilization efficiency of PGA on glyoxyl agarose and the catalytic properties of the PGA derivative, although it impaired the posttranslational steps of overexpressed protein maturation.
Scaramozzino
Francesca
F
Dipartimento di Genetica e Microbiologia, Università degli Studi di Pavia, Via Ferrata 1, 27100 Pavia, Italy.
Estruch
Ilona
I
Rossolillo
Paola
P
Terreni
Marco
M
Albertini
Alessandra M
AM
D001483:Base Sequence; D002384:Catalysis; D003001:Cloning, Molecular; D017931:DNA Primers; D004800:Enzymes, Immobilized / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D007202:Indicators and Reagents; D007700:Kinetics; D016297:Mutagenesis, Site-Directed; D009842:Oligopeptides; D010399:Penicillin Amidase / Q000378:metabolism*; D016133:Polymerase Chain Reaction; D011994:Recombinant Proteins / Q000378:metabolism
D017931:DNA Primers; D004800:Enzymes, Immobilized; D007202:Indicators and Reagents; D009842:Oligopeptides; D011994:Recombinant Proteins; D010399:Penicillin Amidase