BTD

BTD

Target · Secreted enzyme

BTD Biotinidase

BTD (biotinidase) is a secreted hydrolase that releases biotin from biocytin, the product of biotin-dependent carboxylase degradation. By regenerating free biotin, the BTD protein supports biotin recycling, and mutations in the BTD gene are associated with biotinidase deficiency. Browse Assay Genie's current range of BTD research reagents below, or read on for the biology behind the target.

Secreted, extracellular spaceBiotin-recycling hydrolaseLinked to biotinidase deficiency
523 aa
Protein length
~59 kDa
Molecular weight
3p25.1
Gene locus
EC 3.5.1.12
Enzyme class
Target information

What is BTD (biotinidase)?

BTD functions to recycle protein-bound biotin. It catalyses the cleavage of biocytin (biotin-epsilon-lysine), a normal product of the degradation of biotin-dependent carboxylases, and in doing so regenerates free biotin that can be used again. The enzyme has also been shown to have biotinyl transferase activity, in addition to its hydrolytic role.

The enzyme is classified as EC 3.5.1.12 and belongs to the carbon-nitrogen hydrolase superfamily. Within the HGNC classification it sits in the Vanin family, and UniProt places it in the BTD/VNN family. UniProt records its subcellular location as secreted, in the extracellular space. The human BTD gene has orthologues named Btd in both mouse and rat, which allows the biology to be studied in rodent models. Multiple transcript variants encoding different isoforms of the BTD gene have been described.

BTD is best known for its disease relevance: mutations in this gene are associated with biotinidase deficiency. Because the protein's role is defined by the release of biotin from biocytin, it is a natural subject for work on biotin recycling and on the fate of biotin-dependent carboxylases. Researchers studying biotinidase, whether through BTD expression, protein levels or enzymatic activity, will find it a well-defined enzyme with a clear substrate and product.

Biotin recycling

BTD cleaves biocytin to regenerate free biotin, making it central to studies of how protein-bound biotin is recycled.

Biotinidase deficiency research

Mutations in the BTD gene are associated with biotinidase deficiency, so the protein is a focus for studying this condition.

Carboxylase degradation studies

Biocytin is a normal product of biotin-dependent carboxylase degradation, and BTD acts on it, linking the enzyme to carboxylase turnover.

Hydrolase and Vanin family biology

As a member of the carbon-nitrogen hydrolase superfamily and the BTD/VNN family, BTD offers a reference point for comparative enzyme studies.

Background

BTD frequently asked questions

What does BTD do?

BTD, or biotinidase, catalyses the release of biotin from biocytin, which is produced when biotin-dependent carboxylases are degraded. This regenerates free biotin and recycles protein-bound biotin. The enzyme has also been shown to have biotinyl transferase activity.

Does BTD have other names or isoforms?

No alternative symbols or previous names are listed for BTD in HGNC, where the full name is biotinidase. NCBI Gene reports that multiple transcript variants encoding different isoforms have been described. It belongs to the Vanin family and the BTD/VNN family.

Is BTD linked to disease and conserved in rodents?

Mutations in the BTD gene are associated with biotinidase deficiency. Orthologues named Btd exist in both mouse and rat. Check the datasheet of any product for its validated reactivity before using it with a particular species.

Explore

Related targets

Other Vanin family members and biotin-metabolism proteins that are related to BTD.

Gene and protein annotations from HGNC, NCBI Gene and UniProt P43251; product specifications from Assay Genie datasheets.

BTD Product listing