This therapeutic role is not related to prolyl isomerase activity.

The systematic name of this enzyme class is benzyl-thiocyanate isomerase.

Several cases of glucose phosphate isomerase deficiency have recently been identified.

Some of these proteins are highly specific in their function, such as protein disulfide isomerase.

In another approach a bacterial xylose isomerase was introduced.

The structure of triose phosphate isomerase contributes to its function.

M6P is converted to fructose 6-phosphate by mannose phosphate isomerase.

It is sometimes referred to as "glucose isomerase".

Prolyl isomerase activity was first discovered using a chymotrypsin-based assay.

This enzyme belongs to the isomerase family which acts on carbohydrates and their derivatives.

This isomerase activity can be inhibited by immunosuppressive drugs.

Other names in common use include rhamnose isomerase, and L-rhamnose ketol-isomerase.

The only known naturally occurring genetic mutation results in ribose-5-phosphate isomerase deficiency, discussed below.

The critical enzyme step is two-fold using a 3-beta-hydroxysteroid dehydrogenase and a delta 4-5 isomerase.

With a single diagnosed patient only, ribose-5-phosphate isomerase deficiency is presently considered the rarest genetic disease.

The structure is named after triosephosphate isomerase, a conserved metabolic enzyme.

Chalcone isomerase is responsible for their conversion into flavanones and other flavonoids.

Odd-numbered double bonds are handled by the isomerase.

This enzyme is also called prostaglandin A isomerase.

Rpe65 is the retinoid isomerase in bovine retinal pigment epithelium.

Acceleration of the in vitro folding rate by the addition of a prolyl isomerase.

Tetrahydroxychalcone is then converted into naringenin using chalcone isomerase.

In an immunoblot, antibodies were run against all enoyl CoA isomerase.

This domain has disulphide isomerase activity.

The enzyme chalcone isomerase uses a chalcone-like compound to produce a flavanone.