[ATP-dependent proteinase La from Escherichia coli].
Homogeneous preparations of the ATP-dependent La proteinase from E. coli and two its mutant forms, containing an alanine residue instead of Ser679 or Ser368, were isolated. Ser679 was shown to be catalytically active rather than Ser368 as suggested in the literature. To choose between the alternative structures of the gene lon La proteinase fragments within the controversial regions were analysed and the gene structure established at the Laboratory of Proteolytic Enzymes (Institute of Bioorganic Chemistry) was confirmed. Inactivity of La proteinase in some in vitro systems suggests its functioning in vivo to be not autonomous, requiring additional factors.
Romanova
T V
TV
Kotova
S A
SA
Amerik
A Iu
AIu
Lykov
I P
IP
Ginodman
L M
LM
Antonov
V K
VK
D049069:ATP-Dependent Proteases; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000595:Amino Acid Sequence; D001665:Binding Sites; D002384:Catalysis; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D008969:Molecular Sequence Data; D009154:Mutation; D049070:Protease La; D012697:Serine Endopeptidases / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*
D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D049069:ATP-Dependent Proteases; D012697:Serine Endopeptidases; C483567:Lon protein, E coli; D049070:Protease La; D000251:Adenosine Triphosphatases
ATP-zavisimaia proteinaza La iz Escherichia coli.