Hydroxyacid oxidase (glycolate oxidase) 1

HAO1

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2NZL, 2RDT, 2RDU, 2RDW, 2W0U

Identifiers

Aliases

HAO1, GOX, GOX1, HAOX1, Hydroxyacid oxidase (glycolate oxidase) 1, hydroxyacid oxidase 1, GO

External IDs

OMIM: 605023 MGI: 96011 HomoloGene: 6578 GeneCards: HAO1

Gene location (Human)

Chr.	Chromosome 20 (human)^[1]

Band	20p12.3	Start	7,882,985 bp^[1]
Band	20p12.3	End	7,940,458 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 2 (mouse)^[2]

Band	2 F2\|2 65.65 cM	Start	134,339,281 bp^[2]
Band	2 F2\|2 65.65 cM	End	134,396,288 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

right lobe of liver

islet of Langerhans

kidney

kidney

gallbladder

renal cortex

body of pancreas

blood

intestinal epithelium

small intestine

Top expressed in

left lobe of liver

sexually immature organism

spermatid

blastocyst

ureter

atrioventricular valve

thoracic diaphragm

pancreas

islet of Langerhans

pituitary gland

More reference expression data

BioGPS

n/a

Gene ontology
Molecular function	(S)-2-hydroxy-acid oxidase activity oxidoreductase activity FMN binding signaling receptor binding catalytic activity glyoxylate oxidase activity
Cellular component	peroxisome peroxisomal matrix cytosol
Biological process	fatty acid alpha-oxidation response to oxidative stress glycolate catabolic process cellular nitrogen compound metabolic process protein targeting to peroxisome
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: 134.34 – 134.4 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Hydroxyacid oxidase (glycolate oxidase) 1 is a protein that in humans is encoded by the HAO1 gene.^[5]

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. 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]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000101323 - Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000027261 - Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b "Entrez Gene: Hydroxyacid oxidase (glycolate oxidase) 1".
^ Woolf, Alan D.; Wynshaw-Boris, Anthony; Rinaldo, Piero; Levy, Harvey L. (March 1992). "Intentional infantile ethylene glycol poisoning presenting as an inherited metabolic disorder". The Journal of Pediatrics. 120 (3): 421–424. doi:10.1016/s0022-3476(05)80910-2. ISSN 0022-3476. PMID 1538289.

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. 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. S2CID 83505835.
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. 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.

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This page was last edited on 18 August 2023, at 22:19

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Function

References

Further reading