Inhibition kinetics of green crab (Scylla serrata) alkaline phosphatase by zinc ions: a new type of complexing inhibition.
The Tsou method was used to study the kinetic course of inactivation of green crab alkaline phosphatase by zinc ions. The results show that the enzyme was inactivated by a complexing scheme which has not been previously identified. The enzyme first reversibly and quickly binds Zn(2+) and then undergoes a slow reversible course to inactivation and slow conformational change. The inactivation reaction is a single molecule reaction and the apparent inactivation rate constant is for a saturated reaction being independent of Zn(2+) concentration if the concentration is sufficiently high. The microscopic rate constants of inactivation and the association constant were determined from the measurements.
Zhang
R Q
RQ
Department of Biological Science and Biotechnology, Center for Ocean Science and Engineering, Tsinghua University, Beijing, China.
Chen
Q X
QX
Xiao
R
R
Xie
L P
LP
Zeng
X G
XG
Zhou
H M
HM
D000469:Alkaline Phosphatase / Q000037:antagonists & inhibitors* / Q000737:chemistry; D000814:Aniline Compounds / Q000494:pharmacology; D000818:Animals; D003386:Brachyura / Q000201:enzymology*; D004305:Dose-Response Relationship, Drug; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D007700:Kinetics; D009943:Organophosphorus Compounds / Q000494:pharmacology; D011487:Protein Conformation / Q000187:drug effects; D019345:Zinc Acetate / Q000494:pharmacology*
D000814:Aniline Compounds; D004791:Enzyme Inhibitors; D009943:Organophosphorus Compounds; C068798:4-aminophenylphosphate; D000469:Alkaline Phosphatase; D019345:Zinc Acetate