Kinetics of inhibition of alkaline phosphatase from green crab (Scylla serrata) by N-bromosuccinimide.
The inactivation of alkaline phosphatase from green crab (Scylla serrata) by N-bromosuccinimide has been studied using the kinetic method of the substrate reaction during modification of enzyme activity previously described by Tsou [(1988), Adv. Enzymol. Related Areas Mol. Biol. 61, 381-436]. The results show that inactivation of the enzyme is a slow, reversible reaction. The microscopic rate constants for the reaction of the inactivator with free enzyme and the enzyme-substrate complex were determined. Comparison of these rate constants indicates that the presence of substrate offers marked protection of this enzyme against inactivation by N-bromosuccinimide. The above results suggest that the tryptophan residue is essential for activity and is situated at the active site of the enzyme.
Chen
Q X
QX
Department of Biology, Xiamen University, China.
Zhang
W
W
Zheng
W Z
WZ
Zhao
H
H
Yan
S X
SX
Wang
H R
HR
Zhou
H M
HM
D000469:Alkaline Phosphatase / Q000037:antagonists & inhibitors*; D000818:Animals; D001665:Binding Sites; D003386:Brachyura / Q000201:enzymology*; D001974:Bromosuccinimide / Q000494:pharmacology; D007700:Kinetics; D008956:Models, Chemical; D009596:Nitrophenols / Q000378:metabolism / Q000494:pharmacology; D009943:Organophosphorus Compounds / Q000378:metabolism / Q000494:pharmacology; D014364:Tryptophan / Q000737:chemistry / Q000378:metabolism
D009596:Nitrophenols; D009943:Organophosphorus Compounds; C008644:nitrophenylphosphate; D014364:Tryptophan; D000469:Alkaline Phosphatase; D001974:Bromosuccinimide