Localization of the potassium ion activation site in human liver fructose 1,6-bisphosphatase.
Three mouse monoclonal antibodies of human liver fructose 1,6-bisphosphatase are shown to bind to the enzyme at different sites as determined by ELISA. The binding of one of the monoclonal antibodies, L2E1, mimics the effects of K+ ions, including increase in the enzyme activity and enhancement of the sensitivity of the enzyme to AMP inhibition. We tentatively suggest that human liver FruP2ase may have a specific K+ activation site, which at least partially overlaps with the L2E1 binding region. This site has been localized by analyzing the peptide fragments formed by cleavage with cyanogen bromide.
Xu
G J
GJ
Shanghai Institute of Biochemistry, Academia Sinica, China.
Yu
Z B
ZB
Hu
G F
GF
Cao
H T
HT
D000911:Antibodies, Monoclonal / Q000378:metabolism*; D004789:Enzyme Activation / Q000187:drug effects; D006597:Fructose-Bisphosphatase / Q000378:metabolism*; D006801:Humans; D008099:Liver / Q000201:enzymology; D010446:Peptide Fragments / Q000378:metabolism*; D011188:Potassium / Q000378:metabolism*; D013329:Structure-Activity Relationship
D000911:Antibodies, Monoclonal; D010446:Peptide Fragments; D006597:Fructose-Bisphosphatase; D011188:Potassium