Ontology highlight
ABSTRACT:
SUBMITTER: Blum MM
PROVIDER: S-EPMC2330113 | biostudies-literature | 2007 Jan
REPOSITORIES: biostudies-literature
Blum Marc-Michael MM Koglin Alexander A Rüterjans Heinz H Schoenborn Benno B Langan Paul P Chen Julian C-H JC
Acta crystallographica. Section F, Structural biology and crystallization communications 20061222 Pt 1
The enzyme diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris is capable of decontaminating a wide variety of toxic organophosphorus nerve agents. DFPase is structurally related to a number of enzymes, such as the medically important paraoxonase (PON). In order to investigate the reaction mechanism of this phosphotriesterase and to elucidate the protonation state of the active-site residues, large-sized crystals of DFPase have been prepared for neutron diffraction studies. Available H a ...[more]