This enzyme belongs to the family of isomerases, specifically intramolecular lyases.

This enzyme removes the C(7-8) double bond introduced by the sterol delta8-delta7 isomerases.

Isomerases can be further classified into six subclasses:

This enzyme belongs to the family of isomerases, to be specific those racemases and epimerases acting on other compounds.

The sequence around the active site residues is conserved in all known triose phosphate isomerases.

EC 5.99 includes other isomerases (including topoisomerases)

Enoyl-CoA isomerases can be categorized into three classes:

DsbC is a prokaryotic disulfide bond isomerases.

Isomerases have their own EC classification of enzymes: EC 5.

This enzyme belongs to the family of isomerases, specifically the phosphotransferases (phosphomutases), which transfer phosphate groups within a molecule.

Human genes encoding Protein disulfide isomerases include:

However, two of these isomerases had antibody attachment: the short chain isomerase and the peroxisomal multifunctional enzyme.

This suggests that they function as thiol-disulfide isomerases involved in disulfide bond formation in the endoplasmic reticulum.

In several of the omega-agatoxins contain one or more D-amino acids which are produced from L-amino acids through the action of peptide isomerases.

Isomerases have been identified that catalyze the interconversion of disulfide species, accelerating the formation of the native disulfide species.

Furthermore, some prolyl isomerases have a degree of sequence specificity and therefore may not catalyze the isomerization of prolines in certain sequence contexts.

The enzyme is a hexamer, forming the largest structurally known ketol isomerase, and has no sequence or structural similarity with other ketol isomerases.

All organisms possess prolyl isomerase enzymes to catalyze this isomerization, and some bacteria have specialized prolyl isomerases associated with the ribosome.

It is a member or a larger class of isomerases which catalyze the interconversion of chemical isomers (in this case structural isomers of pentose).

Protein disulfide isomerases catalyze the proper formation of disulfide bonds; the cell transfers dehydroascorbic acid to the endoplasmic reticulum, which oxidises the environment.

The classes of enzymes that have manganese cofactors are very broad, and include oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases, lectins, and integrins.

This enzyme belongs to the family of isomerases, specifically those other isomerases sole sub-subclass for isomerases that do not belong in the other subclasses.

The names of isomerases are formed as "substrate isomerase" (for example, enoyl CoA isomerase), or as "substrate type of isomerase" (for example, phosphoglucomutase).

Enzymes with single-substrate mechanisms include isomerases such as triosephosphateisomerase or bisphosphoglycerate mutase, intramolecular lyases such as adenylate cyclase and the hammerhead ribozyme, an RNA lyase.

The synthesized PGH2 is converted to prostaglandins (PGD2, PGE2, PGF), prostacyclin (PGI2), or thromboxane A2 by tissue-specific isomerases.