HAO1 Protein, Human (Trx-His)

HAO1 Protein exhibits broad substrate specificity as an (S)-2-hydroxy-acid oxidase, with a notable preference for glycolate oxidation. This enzymatic activity generates glyoxylate, a crucial precursor utilized by alanine-glyoxylate aminotransferase in the peroxisomal synthesis of glycine. This pathway plays a vital role in detoxifying glyoxylate, preventing its accumulation, which could otherwise lead to the formation of kidney stones. Additionally, HAO1 can catalyze the oxidation of glyoxylate and long-chain hydroxyacids, such as 2-hydroxyhexadecanoate and 2-hydroxyoctanoate, albeit with lower catalytic efficiency. While active in vitro with the artificial electron acceptor 2,6-dichlorophenolindophenol (DCIP), it is believed that O2 serves as the physiological electron acceptor, leading to the production of H2O2. Notably, HAO1 does not exhibit activity on L-lactate and 2-hydroxybutanoate. This multifaceted enzymatic functionality underscores its importance in diverse metabolic pathways.