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Biochemistry · Enzymology

Biotin

Biotinum

Biotin is a crucial biologically active substance that acts as a coenzyme for enzymes of the ligase class. In the body, it ensures the flow of energy-dependent carboxylation reactions, being responsible for the binding and transfer of carbon dioxide to a substrate.

Precursor vitaminsVitamin H, Vitamin B7, Biotin itself
Enzyme classLigases (subclass: carboxylases)
Mechanism of actionCarboxylation (addition of a CO₂ molecule)
Energy dependenceThe reaction requires the expenditure of ATP energy
Active formN-carboxybiotin (carbon dioxide on the imidazole ring)
4 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

Role in the body and precursor vitamins

Biotin functions in the biochemical processes of the body primarily as a coenzyme. This means that to perform its task, it must be physically bound to the enzyme molecule, forming a single catalytic apparatus. In biochemical and medical literature, the precursor vitamins of this coenzyme are conventionally considered to be biotin itself, along with its traditional synonyms: vitamin H and vitamin B7.

Upon entering the body, these substances undergo the necessary transformation pathway to integrate into the active sites of specific enzyme proteins. It is important to understand that without a reliable bond with the enzyme, biotin is unable to carry out its coenzymatic functions.

Enzyme class: ligases and carboxylases

In the global international classification of enzymes, biotin is strictly associated with a class called ligases. The main task of ligases in biochemistry is joining two molecules together through the formation of new chemical bonds.

In the case of biotin, we are talking about a narrower and more specialized subclass of ligases — carboxylases. As the name of this subclass implies, carboxylases specialize in one specific chemical operation: they attach a carbon dioxide molecule ($CO_2$) to a target substrate. This fundamental biochemical process is called carboxylation. A critical condition for such reactions to occur is the mandatory presence of an energy source. In this case, the universal energy source is the ATP (adenosine triphosphate) molecule.

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Subtleties of the chemical mechanism

The mechanism of action of biotin-dependent carboxylases is a strict sequence of steps aimed at activating carbon dioxide and its subsequent transfer.

The chemical reaction begins with the carbon dioxide molecule ($CO_2$) transitioning into its active form. This step is inextricably linked to the cleavage and expenditure of energy from an ATP molecule. Then, the activated carbon dioxide binds directly to the coenzyme molecule. A strictly defined nitrogen atom serves as the attachment point. This nitrogen atom is located within the cyclic structure of the biotin molecule, which is called the imidazole ring.

Formation of the active form: N-carboxybiotin

The result of the successful interaction between the biotin molecule and activated carbon dioxide is the formation of a new structural complex — N-carboxybiotin (sometimes referred to simply as carboxybiotin in diagrams).

It is important to be able to distinguish this coenzyme from other well-known coenzymes, such as thiamine pyrophosphate, tetrahydrofolate, or pyridoxal phosphate, which perform entirely different chemical functions in the cell. N-carboxybiotin should also be distinguished from molecules like carbamoyl phosphate or oxybiotin.

The formation of N-carboxybiotin can be represented as a simple yet concise chemical equation: Biotin + $CO_2$ + ATP $\rightarrow$ Carboxybiotin

It is precisely in the form of N-carboxybiotin that the coenzyme is able to act as a reliable donor of the carbon dioxide molecule, successfully completing the carboxylation reaction.

Briefly: answers to topical questions

Which specific biotin-dependent enzymes function in human metabolism?

The following biotin-dependent enzymes from the ligase class (carboxylase subclass) function in human metabolism:

  • Pyruvate carboxylase — participates in gluconeogenesis (conversion of pyruvate to oxaloacetate).
  • Acetyl-CoA carboxylase — ensures the synthesis of fatty acids.
  • Propionyl-CoA carboxylase — ensures the oxidation of propionic acid residues in the Krebs cycle.

Coenzyme biotin in their active centers covalently binds to the ε-amino group of lysine, catalyzing carbon dioxide addition reactions with the expenditure of ATP.

Which protein acts as a natural antivitamin for biotin and prevents its absorption?

The natural antivitamin for biotin is avidin.

Avidin is a chicken egg white glycoprotein found in raw egg white. It forms a specific complex with biotin and converts it into an insoluble, unabsorbable state, reducing biotin absorption. Consuming large amounts of raw egg white can lead to biotin deficiency. During heat treatment, avidin denatures and is destroyed.

What are the clinical manifestations of hypovitaminosis H (biotin)?

Clinical manifestations of biotin deficiency include:

  • Dermatological: dermatitis with excessive sebaceous gland production (seborrhea), hair loss (alopecia), brittle nails.
  • Muscular: myalgia.
  • Hematological: various types of anemia.
  • Neurological: clinical depression.

What is the biochemical difference between the functions of biotin and tetrahydrofolate?

The main biochemical difference between the functions of biotin and tetrahydrofolate lies in the types of transferred groups and enzyme classes.

CharacteristicBiotinTetrahydrofolate (THF)
Enzyme classLigases, carboxylase subclassTransferases, methyltransferases
Main functionSubstrate carboxylation, CO₂ addition; tissue assimilation of carbon dioxide/bicarbonate ionsTransfer of single-carbon fragments
Transferred groupsCO₂Methyl, methylene, formyl, and other single-carbon fragments
Coenzyme formN⁵-carboxybiotin; biotin is bound to the ε-NH₂ group of lysine in the active center of "biotin" enzymesCoenzyme forms of THF: N⁵-formyl-THF, N¹⁰-formyl-THF, N⁵,N¹⁰-methenyl-THF, N⁵,N¹⁰-methylene-THF, N⁵-methyl-THF
How to memorize

To remember the core mechanism, use the rule of three "C"s: Coenzyme biotin helps carboxylases transform substrates by forming N-carboxybiotin.

Class and exam questions

To which enzyme class and subclass does biotin belong as a coenzyme?

Biotin is a coenzyme for enzymes belonging to the class of ligases. Within this class, it specifically works with the subclass of carboxylases, which catalyze carbon dioxide addition reactions.

Why is an ATP molecule required in reactions involving biotin?

Carbon dioxide addition reactions require energy expenditure. The ATP molecule is necessary to supply the process with energy, allowing the reaction to proceed successfully and form a bond between $CO_2$ and biotin.

What is the active form of biotin called, and where is carbon dioxide fixed within it?

The active form is called N-carboxybiotin. In this structure, the $CO_2$ molecule attaches to one of the nitrogen atoms located in the imidazole ring of biotin.

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What else to study on this topic

  • Detailed chemical structure of the imidazole ring of the biotin molecule.
  • Comparative characteristics of biotin and other coenzymes (thiamine pyrophosphate, tetrahydrofolate, pyridoxal phosphate).
  • Energy balance of the reaction: the exact mechanism of ATP hydrolysis during the formation of carboxybiotin.
  • The mechanism of transfer of activated $CO_2$ from the N-carboxybiotin structure to the final target substrate.

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