Probing the Peripheral Site of Human Butyrylcholinesterase

Probing the Peripheral Site of Human Butyrylcholinesterase

Acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) catalyze the hydrolysis of the neurotransmitter acetylcholine and, thereby, function as coregulators of cholinergic neurotransmission. For both enzymes, hydrolysis takes place near the bottom of a 20 Å deep active site gorge. A number of amino acid residues within the gorge have been identified as important in facilitating efficient ...

PROBING THE ACTIVE SITE OF RHODANESE WITH DISULFIDE REAGENTS

probing the active site of rhodanese with disulfide reagents

0

Structural analysis of human glycoprotein butyrylcholinesterase using atomistic molecular dynamics: The importance of glycosylation site ASN241

Human butyrylcholinesterase (BChE) is a glycoprotein capable of bioscavenging toxic compounds such as organophosphorus (OP) nerve agents. For commercial production of BChE, it is practical to synthesize BChE in non-human expression systems, such as plants or animals. However, the glycosylation profile in these systems is significantly different from the human glycosylation profile, which could ...

Probing the Binding of Valacyclovir Hydrochloride to the Human Serum Albumin

UV-visible and Fluorescence spectroscopic methods were employed to study the interaction of human serum albumin (HSA) with Valacyclovir Hydrochloride. Additionally, molecular dynamics and molecular docking simulations were used to visualize and specify the binding site of Valacyclovir Hydrochloride. The Stern-Volmer and van't Hoff equations along with spectroscopic observations, were used to de...