Lignin inhibits (ADP-ribose)n glycohydrolase activity.
(ADP-ribose)n glycohydrolase activity was inhibited in vitro by lignin, a naturally occurring polymethoxyphenolic compound. However, coniferyl alcohol, which is a main component of lignin, was not inhibitory even at 100 micrograms/ml. Lignin caused competitive inhibition with respect to the substrate (ADP-ribose)n and its Ki value was 18 micrograms/ml. These results suggest that lignin with a polymerized structure has a functional domain that interacts with the (ADP-ribose)n glycohydrolase molecule at the same site as (ADP-ribose)n.
Tanuma
S
S
Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, Teikyo University, Kanagawa, Japan.
Tsai
Y J
YJ
Sakagami
H
H
Konno
K
K
Endo
H
H
D001667:Binding, Competitive; D006026:Glycoside Hydrolases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D007700:Kinetics; D008031:Lignin / Q000494:pharmacology*; D015394:Molecular Structure; D010636:Phenols / Q000494:pharmacology
D010636:Phenols; D008031:Lignin; C010559:coniferyl alcohol; D006026:Glycoside Hydrolases; C022407:poly ADP-ribose glycohydrolase