sialidase

The enzymatic mechanism of influenza virus sialidase has been studied by Taylor et al, shown in Figure 1.

After the Neu5Gc has entered the cell via pinocytosis, the molecule is released by lysosomal sialidase.

Other diseases that result from a deficiency in the sialidase enzyme are categorized in a broader group known as sialidoses.

Other names in common use include N-acetylneuraminate acetyltransferase, sialate 9(4)-O-acetylesterase, and sialidase.

The drugs block sialidase, an enzyme that sits on the surface of the influenza virus and is thought to help newly synthesized viruses push their way out of cells.

One is the lectin haemagglutinin protein with three relatively shallow sialic acid-binding sites and the other is enzyme sialidase with the active site in a pocket.

This enzyme, then referred to as the "receptor-destroying enzyme" was later shown to be the influenza neuraminidase, another viral envelope glycoprotein, which acts as a sialidase.

In the case of nerve damage, research is currently being undertaken at Johns Hopkins University to make damaged nerves in the human body regrow using the enzyme sialidase.

At least four mammalian sialidase homologs have been described in the human genome (see NEU1, NEU2, NEU3, NEU4).

S and s antigens are not affected by treatment with trypsin or sialidase but are destroyed or much depressed by treatment with papain, pronase or alpha-chymotrypsin.

Mucolipidosis type I (ML I) or sialidosis is an inherited lysosomal storage disease that results from a deficiency of the enzyme alpha-N -acetyl neuraminidase (sialidase).

The role of sialidase is to remove a particular form of sialic acid (a sugar molecule) from sugar-protein complexes (referred to as glycoproteins), which allows the cell to function properly.

If a safe pharmacological treatment can be developed - one that increases expression of lysosomal sialidase in neurons without other toxicity - then this new form of therapy could essentially cure the disease.

One experiment has demonstrated that, by using the enzyme sialidase, the genetic defect can be effectively bypassed and GM2 gangliosides can be metabolized so that they become almost inconsequential.

The first step involves the distortion of the α-sialoside from a C chair conformation (the lowest-energy form in solution) to a pseudoboat conformation when the sialoside binds to the sialidase.

Amino Acids Responsible for the Absolute Sialidase Activity of the Influenza A Virus Neuraminidase: Relationship to Growth in Duck Intestine.

Sialidase 1 (lysosomal sialidase), also known as NEU1 is a mammalian lysosomal neuraminidase enzyme which in humans is encoded by the NEU1 gene.

Because of the relative deep active site in which low-molecular-weight inhibitors can make multiple favorable interactions and approachable methods of designing transition-state analogues in the hydrolysis of sialosides, the sialidase becomes more attractive anti-influenza drug target than the haemagglutinin.

Computer Search for Drugs Because the crystal structure of sialidase had previously been determined, Dr. von Itzstein and his colleagues were able to use computer modeling to look for drugs that matched the enzyme's configuration, fitting it like a glove and blocking it from acting.