Hydroxyacid oxidase (glycolate oxidase) 1

Hydroxyacid oxidase (glycolate oxidase) 1
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2NZL​, 2RDT​, 2RDU​, 2RDW​, 2W0U​
Identifiers
Symbols	HAO1 ; GOX; GOX1; HAOX1
External IDs	OMIM: 605023 HomoloGene: 6578 GeneCards: HAO1 Gene
EC number	1.1.3.15
Gene ontology Molecular function • (S)-2-hydroxy-acid oxidase activity • receptor binding • glycolate oxidase activity • FMN binding • glyoxylate oxidase activity • very-long-chain-(S)-2-hydroxy-acid oxidase activity • long-chain-(S)-2-hydroxy-long-chain-acid oxidase activity • medium-chain-(S)-2-hydroxy-acid oxidase activity Cellular component • peroxisome • peroxisomal matrix Biological process • fatty acid alpha-oxidation • response to oxidative stress • cellular nitrogen compound metabolic process • small molecule metabolic process • glycolate catabolic process • glyoxylate metabolic process Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	54363	15112
Ensembl	ENSG00000101323	ENSMUSG00000027261
UniProt	Q9UJM8	Q9WU19
RefSeq (mRNA)	NM_017545	NM_010403
RefSeq (protein)	NP_060015	NP_034533
Location (UCSC)	Chr 20: 7.88 – 7.94 Mb	Chr 2: 134.5 – 134.55 Mb
PubMed search

Hydroxyacid oxidase (glycolate oxidase) 1 is a protein that in humans is encoded by the HAO1 gene.^[1]

Function

This gene is one of three related genes that have 2-hydroxyacid oxidase 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. 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.^[1]

References

1. "Entrez Gene: Hydroxyacid oxidase (glycolate oxidase) 1".

Further reading

• Bourhis JM, Vignaud C, Pietrancosta N, Guéritte F, Guénard D, Lederer F, Lindqvist Y (2009). "Structure of human glycolate oxidase in complex with the inhibitor 4-carboxy-5-(4-chlorophenyl)sulfanyl-1,2,3-thiadiazole". Acta Crystallographica Section F Structural Biology and Crystallization Communications 65 (Pt 12): 1246–53. doi:10.1107/S1744309109041670. PMC 2802872. PMID 20054120.
• Jones JM, Morrell JC, Gould SJ (2000). "Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases". The Journal of Biological Chemistry 275 (17): 12590–7. doi:10.1074/jbc.275.17.12590. PMID 10777549.
• Murray MS, Holmes RP, Lowther WT (2008). "Active site and loop 4 movements within human glycolate oxidase: Implications for substrate specificity and drug design". Biochemistry 47 (8): 2439–49. doi:10.1021/bi701710r. PMC 2683390. PMID 18215067.
• Lan S, Wang H, Jiang H, Mao H, Liu X, Zhang X, Hu Y, Xiang L, Yuan Z (2003). "Direct interaction between α-actinin and hepatitis C virus NS5B". FEBS Letters 554 (3): 289–94. doi:10.1016/S0014-5793(03)01163-3. PMID 14623081.
• Williams E, Cregeen D, Rumsby G (2000). "Identification and expression of a cDNA for human glycolate oxidase". Biochimica et Biophysica Acta 1493 (1-2): 246–8. doi:10.1016/s0167-4781(00)00161-5. PMID 10978532.
• 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. PMID 21141873.
• 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. PMID 17669354.
• Danpure CJ (2005). "Primary hyperoxaluria: From gene defects to designer drugs?". Nephrology Dialysis Transplantation 20 (8): 1525–1529. doi:10.1093/ndt/gfh923. PMID 15956068.
• 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. PMID 20189245.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.