[Suc-Phe-Leu-Phe-SBzl--a new substrate for functional study of Escherichia coli ATP-dependent Lon-proteinase and its modified forms].
A new efficient substrate, Suc-Phe-Leu-Phe-SBzl, was proposed for studying the function of the Escherichia coli ATP-dependent Lon protease and its modified forms. The kinetic parameters of hydrolysis of the substrate were determined. The esterase activity of protease Lon was found to be nucleotide-regulated.
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
E E
EE
Mel'nikov
K B
KB
Tsirul'nikov
F S
FS
Rasulova
L M
LM
Ginodman
T V
TV
Rotanova
D049069:ATP-Dependent Proteases; D000255:Adenosine Triphosphate / Q000737:chemistry*; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000235:genetics; D006868:Hydrolysis; D007700:Kinetics; D009154:Mutation; D009842:Oligopeptides / Q000737:chemistry*; D049070:Protease La; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000235:genetics; D013379:Substrate Specificity
D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D009842:Oligopeptides; C115477:succinylphenylalanyl-leucyl-phenylalanine thiobenzylate; D000255:Adenosine Triphosphate; D049069:ATP-Dependent Proteases; D012697:Serine Endopeptidases; C483567:Lon protein, E coli; D049070:Protease La
Suc-Phe-Leu-Phe-SBzl--novyĭ substrat dlia issledovaniia funktsionirovaniia ATP-zavisimoĭ Lon-proteinazy Escherichia coli i ee modifitsirovannykh form.