Stabilization of luciferase intermediates by fatty amines, amides, and nitriles.
Long-chain aliphatic amides, mono- and diamines, mono- and dialcohols, and nitriles were found to inhibit the bacterial luciferase reaction by binding with an enzyme intermediate (II, the luciferase-bound 4 alpha-flavin hydroperoxide). Inhibition was determined by measuring the decay rates of the inhibitor-intermediate II complex at different inhibitor concentrations. The data fit a model which was used to estimate the KI. At high concentrations, a plot of the decay rate (k) vs 1/[I] produced a straight line; extrapolation of this to 1/[I] = 0 yields an estimate of the decay rate at infinite inhibitor concentration which we defined as the inhibitor-enzyme-substrate stabilization constant, kESI.
Makemson
J C
JC
Department of Biological Sciences, Florida International University, Miami, Florida 33199.
Hastings
J W
JW
Quirke
J M
JM
D000438:Alcohols / Q000494:pharmacology; D000577:Amides / Q000494:pharmacology*; D000588:Amines / Q000494:pharmacology*; D007700:Kinetics; D008156:Luciferases / Q000302:isolation & purification / Q000378:metabolism*; D009570:Nitriles / Q000494:pharmacology*; D013329:Structure-Activity Relationship; D014733:Vibrio / Q000201:enzymology
D000438:Alcohols; D000577:Amides; D000588:Amines; D009570:Nitriles; D008156:Luciferases; C003935:dodecylamine