It has been classified both as a ligase and a lyase.

The systematic name of this enzyme class is heparin-sulfate lyase.

Other names in common use include benzaldehyde lyase, and 2-hydroxy-1,2-diphenylethanone benzaldehyde-lyase.

Xanthan lyase was first identified and partially purified in 1987.

It is also known as cyanate lyase or cyanase.

This enzyme is a member of the aromatic amino acid lyase family.

A hemithioacetal is also invoked in the mechanism of prenylcysteine lyase.

The only route by which sphingolipids are converted to non-sphingolipids is through sphingosine-1-phosphate lyase.

For example, an enzyme that catalyzed this reaction would be a lyase:

However, alternate pathways have been proposed in organisms lacking isocitrate lyase.

Phenylalanine ammonia lyase can perform different functions in different species.

Isocitrate lyase family is a family of evolutionarily related proteins.

This enzyme is also called D-tagatose-1,6-bisphosphate triosephosphate lyase.

It also induces the expression of Pyruvate formate lyase.

The enzyme is a member of the ammonia lyase family, which cleaves carbon-nitrogen bonds.

The 8 kDa domain has lyase activity that can remove a 5' deoxyribosephosphate group from the end of a strand break.

Methylisocitrate lyase was discovered in 1976.

The fold resembles that of N-acetylneuraminate lyase.

Lactoylglutathione lyase in humans is encoded by the GLO1 gene.

The enzyme is considered a phosphorus-oxygen lyase.

The monomer of adenylosuccinate lyase has three domains.

Adenylosuccinate lyase mutants can have considerably reduced activity whether the mutation is in or away from the active site.

This step is catalyzed by adenylosuccinate lyase.

Dichloromethane dehalogenase is a lyase enzyme which generates formaldehyde.

Enolase belongs to the class Lyase.