Modification of catalytic properties of chicken liver fructose 1,6-bisphosphatase by allicin.
The activity of chicken liver fructose 1,6-bisphosphatase increases dramatically after incubation with allicin, a major biologically active compound produced by garlic. Activation is more pronounced when the enzyme is assayed with Mn2+ than Mg2+. Maximum activation is accompanied by the disappearance of 4 highly reactive sulfhydryl groups per molecule of enzyme. This modification also leads to loss of activation by K+, and reduced sensitivity to inhibition by AMP, fructose 2,6-bisphosphate, and high concentration of fructose 1,6-bisphosphate. All the altered properties induced by allicin can be reversed by dithiothreitol or tris(2-carboxyethyl)phosphine, the latter being much more effective.
Han
J
J
Department of Pharmacology and Toxicology, Morehouse School of Medicine, Atlanta, GA 30310.
Lawson
L
L
Chu
T C
TC
Potter
D
D
Han
G
G
Han
P
P
D000818:Animals; D002384:Catalysis; D002645:Chickens; D004220:Disulfides; D004789:Enzyme Activation / Q000187:drug effects; D006597:Fructose-Bisphosphatase / Q000737:chemistry / Q000187:drug effects* / Q000378:metabolism; D066298:In Vitro Techniques; D008099:Liver / Q000187:drug effects / Q000201:enzymology*; D008956:Models, Chemical; D013329:Structure-Activity Relationship; D013438:Sulfhydryl Compounds; D013441:Sulfinic Acids / Q000494:pharmacology*
D004220:Disulfides; D013438:Sulfhydryl Compounds; D013441:Sulfinic Acids; C006452:allicin; D006597:Fructose-Bisphosphatase