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.
Shanghai Institute of Biochemistry, Academia Sinica, China.
G J
GJ
Xu
Z B
ZB
Yu
G F
GF
Hu
H T
HT
Cao
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