Neuraminidase of the serine enzyme

The neuraminidase[,nj of the nerve enzyme?? R? ' M?N?DE?Z]

The enzyme called sialic acid is a glycoprotein distributed on the membrane of influenza virus, it has antigenicity, can catalyze the hydrolysis of sialic acid, help mature influenza virus from host cell infect new cells, play an important role in the life cycle of influenza virus. In the influenza A virus, the antigenic nature of the enzyme mutation, which is the basis for the classification of influenza A virus subtype, there are currently known as influenza A virus in a total of 9 different kinds of neural enzyme anti-enzymatic prototype.

feature editing The histidine-dimer streamer model of the serine enzyme is responsible for catalyzing the hydrolysis of the glucoside bonds between sialic acid and glycoprotein. After the influenza virus infects the host, itsserine enzymesThe surface of the blood coagulation and the host epithelial cells on the surface of the blood coagulation receptor binding, into the cell, the gene using the host cell resources for replication and expression, eventually re-assembled into a new influenza virus particles, in a budding form to highlight the host cell, but the mature influenza virus and host cells, The sialic acid residue, which is still dependent on the end of the blood-clotting molecule, is linked with a sugar group on the surface of the blood-receptor molecule by 2-6 or 2-3 glycosides, which makes the influenza virus unable to immediately disengage from the host cell. The enzyme is responsible for catalyzing the hydrolysis of this important glucoside bond, so that the mature virus particles eventually out of the host cells, infected with new epithelial cells, causing the spread of influenza virus in the patient body.

inhibitorsThe enzyme is one of the targets of influenza therapeutic drugs, since the human understanding of the role of the enzymes began to study the enzyme inhibitor, there are two kinds of neural enzyme inhibitors listed, a three-stage clinical study. Currently in the research of the serine enzyme inhibitor according to the structure can be divided into sialic acid analogues, benzoic acid derivative, cyclohexene derivative, cyclohexane derivatives, pyrrolidine derivatives and natural extracts of six categories. All the four inhibitors were in the conservative sequence of the center of the glutamine-like barrel structure as the site of action. There is a ring-shaped central structure, and the structural-activity relationship shows that the size and saturation of the ring structure have little effect on the activity of the inhibitor, and the configuration and electrical properties of the substituents are the key factors determining the activity of the inhibitor. Currently listed, the arginine inhibitor has GlaxoSmithKline Zanamivir and Roche's oseltamivir.

Neuraminidase of the serine enzyme