Site-directed mutagenesis of La protease. A catalytically active serine residue.
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.
Amerik AYu
Shemyakin Institute of Biorganic Chemistry, USSR Academy of Sciences, Moscow.
Antonov
V K
VK
Gorbalenya
A E
AE
Kotova
S A
SA
Rotanova
T V
TV
Shimbarevich
E V
EV
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
D006360:Heat-Shock Proteins; D012694:Serine; D004262:DNA Restriction Enzymes; D049069:ATP-Dependent Proteases; D012697:Serine Endopeptidases