title: Site-directed mutagenesis of La protease. A catalytically active serine residue.
abstract: Comparative sequence analysis of Escherichia coli ATP-dependent La protease led to the suggestion that Ser679 is the catalytically active enzyme residue. Site-directed mutagenesis Ser679----Ala, investigation of the cells containing the mutant plasmid, and study of the partially purified mutant protein produced results in favour of this suggestion.
authors.affiliation: Shemyakin Institute of Biorganic Chemistry, USSR Academy of Sciences, Moscow.
authors.lastname: Amerik AYu
authors.forename: V K
authors.initials: VK
authors.lastname: Antonov
authors.forename: A E
authors.initials: AE
authors.lastname: Gorbalenya
authors.forename: S A
authors.initials: SA
authors.lastname: Kotova
authors.forename: T V
authors.initials: TV
authors.lastname: Rotanova
authors.forename: E V
authors.initials: EV
authors.lastname: Shimbarevich
mesh_terms: D049069:ATP-Dependent Proteases; D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D003001:Cloning, Molecular; D004262:DNA Restriction Enzymes; D004926:Escherichia coli / Q000201:enzymology*; D006360:Heat-Shock Proteins; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010957:Plasmids; D012694:Serine; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000235:genetics; D014169:Transformation, Bacterial
chemical_list: D006360:Heat-Shock Proteins; D012694:Serine; D004262:DNA Restriction Enzymes; D049069:ATP-Dependent Proteases; D012697:Serine Endopeptidases