Inhibition of phosphofructokinases by copper(II).
The biochemical inhibition by Cu2+ on eight phylogenetically and biochemically different phosphofructokinases (PFKs) was investigated. The enzymes screened included representatives from thermophilic and mesophilic bacteria, a hyperthermophilic archaeon and a eukaryote, covering all three phosphoryl donor subtypes (ATP, ADP and pyrophosphate). The sensitivities of the enzymes to Cu2+ varied greatly, with the archaeal ADP-PFK being the least and the eukaryote ATP-PFK being the most sensitive. The bacterial ATP- and pyrophosphate-dependent PFKs showed intermediate sensitivity with the exception of the Spirochaeta thermophila enzyme (pyrophosphate-dependent) which was relatively resistant.
Gebhard
S
S
Thermophile Research Unit, Department of Biological Sciences, University of Waikato, Private Bag 3105, Hamilton, New Zealand.
Ronimus
R S
RS
Morgan
H W
HW
D000818:Animals; D001419:Bacteria / Q000201:enzymology; D003300:Copper / Q000494:pharmacology*; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D009130:Muscle, Smooth / Q000201:enzymology; D010732:Phosphofructokinase-1 / Q000037:antagonists & inhibitors* / Q000378:metabolism*; D011817:Rabbits; D019712:Thermococcus / Q000201:enzymology
D004791:Enzyme Inhibitors; D003300:Copper; D010732:Phosphofructokinase-1