HAO1 Human

HAO1 catalyzes the oxidation of glycolate to glyoxylate and glyoxylate to oxalate, with the reduction of oxygen to hydrogen peroxide . This enzyme exhibits 2-hydroxyacid oxidase activity and is most active on two-carbon substrates such as glycolate . It can also act on 2-hydroxy fatty acids, with higher activity towards 2-hydroxy palmitate and 2-hydroxy octanoate .

In the context of peroxisomal glyoxylate metabolism, HAO1 is the enzyme upstream of alanine-glyoxylate aminotransferase (AGXT). Mutations in AGXT cause Primary Hyperoxaluria type 1 (PH1), an autosomal recessive disorder characterized by the deposition of insoluble calcium oxalate stones . These stones primarily accumulate in the kidneys, leading to end-stage renal disease, but can also deposit in other tissues such as the heart, nerves, bones, eyes, and bone marrow .

Recombinant HAO1 is produced using expression hosts such as E. coli. The recombinant protein is typically tagged for purification and analysis purposes. For example, a His-tagged recombinant human HAO1 protein has a calculated molecular weight of approximately 58.6 kDa and an observed molecular weight of 56 kDa . The protein is purified to a high degree, with a purity of over 95% as determined by reducing SDS-PAGE .

Recombinant HAO1 is used in research to study its role in metabolic pathways and its potential as a target for therapeutic intervention in metabolic disorders such as PH1 . It is also utilized in various in vitro assays to detect ligand or inhibitor binding and enzyme activity .

Recombinant HAO1 is typically supplied as a filtered solution in phosphate-buffered saline (PBS) at pH 7.4. It is stored at temperatures below -20°C to maintain stability and minimize freeze-thaw cycles .