ALAD
ALAD (aminolevulinate dehydratase, also known as ALADH and PBGS) is a cytosolic enzyme that catalyses an early step in tetrapyrrole biosynthesis. It condenses two molecules of 5-aminolevulinate to form porphobilinogen, a precursor of heme. Browse Assay Genie's current range of ALAD research reagents below, or read on for the biology behind the target.
ALAD catalyses an early step in the biosynthesis of tetrapyrroles. Each subunit binds two molecules of 5-aminolevulinate, each at a distinct site, and catalyses their condensation to form porphobilinogen. Porphobilinogen is a precursor of heme, cytochromes and other hemoproteins. In the porphyrin and heme biosynthetic pathway, ALAD catalyses the second step, and zinc is essential for its enzymatic activity.
The active enzyme is composed of eight identical subunits. ALAD belongs to the ALAD family and is classed by HGNC in the carbon-oxygen lyases gene group, with the EC number 4.2.1.24. UniProt records its subcellular location as the cytosol. The ALAD gene undergoes alternative splicing, which gives rise to multiple transcript variants encoding different isoforms. Mouse and rat each have an orthologous gene, Alad.
ALAD is of interest in toxicology and porphyria research. Its enzymatic activity is inhibited by lead, and a defect in the ALAD structural gene can cause increased sensitivity to lead poisoning and acute hepatic porphyria. The enzyme has also been known as porphobilinogen synthase (PBGS), and earlier HGNC naming was "aminolevulinate, delta-, dehydratase". Researchers studying ALAD often investigate it alongside other heme pathway components, using tools such as an ALAD antibody or ALAD ELISA kit.
ALAD catalyses the second step of the porphyrin and heme pathway, producing porphobilinogen, a precursor of heme, cytochromes and other hemoproteins.
ALAD enzymatic activity is inhibited by lead, and a defect in the gene can increase sensitivity to lead poisoning.
A defect in the ALAD structural gene can cause acute hepatic porphyria, making the enzyme relevant to porphyria research.
The octameric enzyme binds two 5-aminolevulinate molecules per subunit at distinct sites and requires zinc for activity.
ALAD catalyses an early step in tetrapyrrole biosynthesis. It binds two molecules of 5-aminolevulinate per subunit and condenses them to form porphobilinogen, a precursor of heme, cytochromes and other hemoproteins. It acts at the second step of the porphyrin and heme pathway and requires zinc.
ALAD is also called ALADH and PBGS, and the protein is named delta-aminolevulinic acid dehydratase. An earlier HGNC name was aminolevulinate, delta-, dehydratase. Alternative splicing of the gene produces multiple transcript variants that encode different isoforms.
ALAD activity is inhibited by lead, and a defect in the gene can cause increased sensitivity to lead poisoning and acute hepatic porphyria. Mouse and rat both carry an Alad ortholog; check the datasheet of any product for its validated reactivity.
Other heme biosynthesis enzymes and porphyrin pathway targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P13716; product specifications from Assay Genie datasheets.