title: Charge redistribution in adenosylribosyl transferase caused by substitution of a single amino acid residue.
abstract: Dielectric measurements in the frequency range 10(5)-10(8) Hz were performed on wild-type (wt) adenosylribosyl transferase and a mutant enzyme. The analysis of the dielectric relaxation curve allowed the estimation of the hydrodynamic radius and of the electric dipole moment. The first parameter remained unchanged in wt and mutant protein. The dipole moment of the mutant, however, was significantly increased. Implications on the electrostatic interactions between enzyme and substrate are discussed.
authors.affiliation: School of Molecular and Cell Biology, University of Witwatersrand, Johannesburg, South Africa.
authors.forename: Mary
authors.initials: M
authors.lastname: Gianniosis
authors.forename: Valerio
authors.initials: V
authors.lastname: Berardi
authors.forename: Adalberto
authors.initials: A
authors.lastname: Bonincontro
authors.forename: Eric
authors.initials: E
authors.lastname: Dabbs
authors.forename: Gianfranco
authors.initials: G
authors.lastname: Risuleo
mesh_terms: D036002:ADP Ribose Transferases / Q000235:genetics* / Q000378:metabolism*; D000192:Actinomycetales / Q000201:enzymology; D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism; D007700:Kinetics; D016366:Open Reading Frames; D010446:Peptide Fragments / Q000737:chemistry; D016133:Polymerase Chain Reaction
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D010446:Peptide Fragments; D036002:ADP Ribose Transferases