Anti-ALAD antibody [EPR10268(B)]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

The ALAD also known as Aminolevulinate Dehydratase is an essential enzyme involved in the biosynthesis of heme facilitating the condensation of two molecules of aminolevulinic acid to form porphobilinogen. The enzyme has a molecular mass of approximately 36 kDa. It is ubiquitously expressed across various tissues with notable activity in the liver and erythroid precursor cells within the bone marrow where heme biosynthesis is essential for the production of hemoglobin.

Biological function summary

The enzyme plays an important role in the early steps of the heme biosynthetic pathway. ALAD forms part of a multi-step process critical for heme production which is an important component of hemoglobin myoglobin and various cytochromes. The enzyme operates as a metalloenzyme requiring zinc for its activity and is subject to regulation by metal ion availability and substrate concentrations. Alterations in its activity can have significant impacts on cellular iron utilization and red blood cell function.

Pathways

ALAD plays a critical role within the heme biosynthesis pathway linking amino acid metabolism to porphyrin and heme production. It connects tightly with other enzymes involved in this pathway such as porphobilinogen deaminase. ALAD's function ensures the steady supply of intermediates necessary for synthesizing heme which serves further purposes in electron transport and oxygen transport systems within cells.

Associated diseases and disorders

The improper function of ALAD associates with conditions such as lead poisoning and acute intermittent porphyria. In lead poisoning lead ions inhibit ALAD activity resulting in the accumulation of its substrate aminolevulinic acid and subsequent disturbances in heme production. In acute intermittent porphyria mutations in ALAD or interacting proteins like porphobilinogen deaminase can influence enzyme efficiency and increase the risk of metabolic crises. Understanding ALAD's role offers potential therapeutic insights for managing these disorders.