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Biochemistry · Enzymology

Lyases

Lyases

Lyases are enzymes that catalyze the non-hydrolytic removal of various chemical groups from substrates, as well as the addition of molecules across double bonds. The main feature of these biocatalysts is that bond cleavage occurs without the involvement of water as a cleaving agent.

MechanismNon-hydrolytic group removal
GroupsRemoval of $CO_2$, $H_2O$, $NH_2$, $SH_2$, etc.
BondsAddition of molecules across double bonds
CoenzymePyridoxal phosphate (PLP) for decarboxylases
3 min readFor medical studentsUpdated 09/24/2026
Material prepared by WhiteCoat Pro editorial team based on platform study guidesReviewed by medical editor: Aulov A. A., general practitioner · 09/24/2026

Principles of lyase action

These enzymes perform two key, yet functionally opposite tasks. First, they are capable of removing specific groups ($CO_2$, $H_2O$, $NH_2$, $SH_2$) from substrate molecules. A crucial condition is that this occurs via a non-hydrolytic pathway, meaning water does not act as "scissors" (a cleaving agent).

Secondly, lyases can catalyze addition reactions. Most often this involves the addition of a small molecule (such as water) directly across the double bond of the substrate molecule, resulting in a change in its chemical structure.

Decarboxylation reactions

A classic example of group removal is decarboxylation. During this reaction, enzymes remove a carboxyl group (-COOH).

Let's examine this process using a specific example:

  • Substrate: Glutamic acid (also known as glutamate).
  • Enzyme: Glutamate decarboxylase.
  • Coenzyme: Pyridoxal phosphate (PLP).
  • Reaction products: $\gamma$-Aminobutyric acid (GABA) is formed and carbon dioxide ($CO_2$) is released.

Mechanism: The carboxyl group is removed from the $\alpha$-position of glutamic acid. This is precisely how a new molecule is formed through the removal of $CO_2$.

Test your knowledge on this topicTasks from the Biochemistry course bank — instant answer and detailed explanation.

Water addition (hydratase) reactions

The second type of lyase reaction is addition. An example of a hydratase reaction is the interaction of a substrate with a water molecule.

  • Substrate: Fumarate.
  • Enzyme: Fumarate hydratase (or fumarase).
  • Reaction equation: `Fumarate + H₂O` $\rightleftarrows$ `Malate`.

Mechanism: Water is added strictly across the double bond of the fumarate molecule. As a result, the double bond region ($CH=CH$) becomes saturated and converts into a single bond region with a hydroxyl group ($CH_2-CH(OH)$), forming malate. This reaction is reversible.

Briefly: answers to topical questions

To which class of enzymes do lyases belong according to the international classification?

According to the international classification, lyases belong to the fourth class of enzymes. All known enzymes are systematized into six main groups based on the type of catalyzed reaction, with lyases assigned a specific ordinal number.

What is the fundamental difference between lyases and hydrolases?

The fundamental difference lies in the mechanism of chemical bond cleavage and the involvement of water molecules in the catalytic process.

SignLyasesHydrolases
Cleavage mechanismNon-hydrolytic bond cleavageBond cleavage involving water
Reaction typeGroup removal without water or addition across double bondsGroup transfer to water

Which enzyme subclasses belong to lyases besides decarboxylases and hydratases?

Besides decarboxylases and hydratases, sources list the following as important subclasses of lyases:

  • C-C lyases.
  • C-O lyases.
  • C-N lyases.
  • C-S lyases.

Additionally, in the classification, class 4 is designated as lyases (synthases).

In which metabolic pathway does fumarate hydratase operate?

Fumarate hydratase (fumarase) functions in the aspartate-argininosuccinate shunt / cycle of regenerating aspartate from fumarate. [Wait, keeping exact meaning:] functions in the cycle of regenerating aspartate from fumarate. During this process, which is closely coupled with the tricarboxylic acid cycle reactions, this enzyme catalyzes the hydration of fumarate to form malate.

What is the biological role of GABA formed during glutamate decarboxylation?

GABA ($\gamma$-aminobutyric acid), formed during the decarboxylation of glutamic acid, serves as an inhibitory neurotransmitter in higher brain centers.

How to memorize

To remember the core concept, imagine that lyases are "dry scissors" (cleaving groups without water) or "glue for double bonds" (adding molecules across a double bond).

Class and exam questions

Do lyases use water to cleave bonds?

No. Lyases perform the removal of chemical groups ($CO_2$, $NH_2$, etc.) via a non-hydrolytic pathway, meaning water does not participate in the reaction as a cleaving agent.

Which group is removed during glutamate decarboxylation?

Upon the action of glutamate decarboxylase, the carboxyl group (-COOH) is removed from the $\alpha$-position of glutamic acid.

How does the bond structure change upon the action of fumarase?

Fumarase adds water across the double bond of fumarate ($CH=CH$). The double bond is broken, and $CH_2-CH(OH)$ is formed — the malate molecule.

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What else to study on this topic

  • Role and functions of $\gamma$-aminobutyric acid (GABA)
  • Structure and functions of the coenzyme pyridoxal phosphate (PLP)
  • Significance of the conversion of fumarate to malate
  • Removal of other groups: ammonia ($NH_2$) and hydrogen sulfide ($SH_2$)

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