This gene is one of three related genes that have 2-hydroxyacidoxidase activity yet differ in encoded protein amino acid sequence, tissue expression and substrate preference. Subcellular location of the encoded protein is the peroxisome. Specifically, this gene is expressed primarily in liver and pancreas and the encoded protein is most active on glycolate, a two-carbon substrate. Glycolate oxidase oxidizes glycolic acid to glyoxylate, and can also oxidize glyoxylate into oxalate. These reactions are central to the toxicity of ethylene glycol poisoning.[6]
The protein is also active on 2-hydroxy fatty acids. The transcript detected at high levels in pancreas may represent an alternatively spliced form or the use of a multiple near-consensus upstream polyadenylation site.[5]
Williams E, Cregeen D, Rumsby G (2000). "Identification and expression of a cDNA for human glycolate oxidase". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1493 (1–2): 246–8. doi:10.1016/s0167-4781(00)00161-5. PMID10978532.
Pennati A, Gadda G (2011). "Stabilization of an intermediate in the oxidative half-reaction of human liver glycolate oxidase". Biochemistry. 50 (1): 1–3. doi:10.1021/bi101387w. PMID21141873.
Vignaud C, Pietrancosta N, Williams EL, Rumsby G, Lederer F (2007). "Purification and characterization of recombinant human liver glycolate oxidase". Archives of Biochemistry and Biophysics. 465 (2): 410–6. doi:10.1016/j.abb.2007.06.021. PMID17669354.
Han S, Lee KM, Park SK, Lee JE, Ahn HS, Shin HY, Kang HJ, Koo HH, Seo JJ, Choi JE, Ahn YO, Kang D (2010). "Genome-wide association study of childhood acute lymphoblastic leukemia in Korea". Leukemia Research. 34 (10): 1271–4. doi:10.1016/j.leukres.2010.02.001. PMID20189245.
