GRHPR

GRHPR
Identifiers
Aliases	GRHPR, GLXR, GLYD, PH2, glyoxylate reductase/hydroxypyruvate reductase, glyoxylate and hydroxypyruvate reductase
External IDs	OMIM: 604296; MGI: 1923488; GeneCards: GRHPR
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2GCG, 2H1S, 2Q50, 2WWR
Enzyme activity
Gene location (Human)
Chr.	Chromosome 9 (human)
End	37,436,990 bp
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)
End	44,990,734 bp
RNA expression pattern
	Top expressed in
	right lobe of liver; ; right adrenal gland; ; left adrenal gland; ; right adrenal cortex; ; left adrenal cortex; ; tendon of biceps brachii; ; human kidney; ; muscle of thigh; ; apex of heart; ; C1 segment;
	Top expressed in
	left lobe of liver; ; right kidney; ; proximal tubule; ; Ileal epithelium; ; human kidney; ; adrenal gland; ; yolk sac; ; cumulus cell; ; epithelium of stomach; ; brown adipose tissue;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	glycerate dehydrogenase activity; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; protein homodimerization activity; NAD binding; carboxylic acid binding; NADP binding; NADPH binding; oxidoreductase activity; hydroxypyruvate reductase activity; glyoxylate reductase (NADP+) activity;
Cellular component	cytoplasm; peroxisomal matrix; extracellular exosome; cytosol;
Biological process	dicarboxylic acid metabolic process; excretion; protein complex oligomerization; metabolism; cellular nitrogen compound metabolic process; glyoxylate metabolic process;
	Sources:Amigo / QuickGO
Orthologs
Databases	NCBI: entry; OMA: entry
	9380
	76238
	ENSG00000137106
	ENSMUSG00000035637
	Q9UBQ7
	Q91Z53
	NM_012203
	NM_080289; NM_001312880
	NP_036335
	NP_001299809; NP_525028
	Wikidata
View/Edit Human	View/Edit Mouse

Glyoxylate reductase/hydroxypyruvate reductase is an enzyme that in humans is encoded by the GRHPR gene.

This gene encodes an enzyme with hydroxypyruvate reductase, glyoxylate reductase, and D-glycerate dehydrogenase enzymatic activities. The enzyme has widespread tissue expression and has a role in metabolism. Type II hyperoxaluria is caused by mutations in this gene. GRHPR mutation analysis needs to pay attention to primer design, because allele dropout can cause false-positive result.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000137106 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000035637 – 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.
↑ Rumsby G, Cregeen DP (Nov 1999). "Identification and expression of a cDNA for human hydroxypyruvate/glyoxylate reductase". Biochim Biophys Acta. 1446 (3): 383–8. doi:10.1016/S0167-4781(99)00105-0. PMID 10524214.
↑ Cramer SD, Ferree PM, Lin K, Milliner DS, Holmes RP (Dec 1999). "The gene encoding hydroxypyruvate reductase (GRHPR) is mutated in patients with primary hyperoxaluria type II". Hum Mol Genet. 8 (11): 2063–9. doi:10.1093/hmg/8.11.2063. PMID 10484776.
1 2 "Entrez Gene: GRHPR glyoxylate reductase/hydroxypyruvate reductase".
↑ Takaoka N, Takayama T, Miyazaki M, Nagata M, Ozono S (Dec 2008). "Modification of primers for GRHPR genotyping: avoiding allele dropout by single nucleotide polymorphisms and homology sequence". Urol Res. 36 (6): 297–302. doi:10.1007/s00240-008-0159-z. PMID 18982322. S2CID 12234158.

External links

GeneReviews/NCBI/NIH/UW entry on Primary Hyperoxaluria Type 2

Takayama T, Nagata M, Ozono S, et al. (2007). "A novel mutation in the GRHPR gene in a Japanese patient with primary hyperoxaluria type 2". Nephrol. Dial. Transplant. 22 (8): 2371–4. doi:10.1093/ndt/gfm271. PMC 2413148. PMID 17510093.
Booth MP, Conners R, Rumsby G, Brady RL (2006). "Structural basis of substrate specificity in human glyoxylate reductase/hydroxypyruvate reductase". J. Mol. Biol. 360 (1): 178–89. doi:10.1016/j.jmb.2006.05.018. PMID 16756993.
Mehrle A, Rosenfelder H, Schupp I, et al. (2006). "The LIFEdb database in 2006". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.
Wiemann S, Arlt D, Huber W, et al. (2004). "From ORFeome to Biology: A Functional Genomics Pipeline". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Lehner B, Sanderson CM (2004). "A Protein Interaction Framework for Human mRNA Degradation". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Simpson JC, Wellenreuther R, Poustka A, et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC 1083732. PMID 11256614.
Hartley JL, Temple GF, Brasch MA (2001). "DNA Cloning Using In Vitro Site-Specific Recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
Webster KE, Ferree PM, Holmes RP, Cramer SD (2000). "Identification of missense, nonsense, and deletion mutations in the GRHPR gene in patients with primary hyperoxaluria type II (PH2)". Hum. Genet. 107 (2): 176–85. doi:10.1007/s004390000351. PMID 11030416. S2CID 10574729.
Huang T, Yang W, Pereira AC, et al. (2000). "Cloning and characterization of a putative human d-2-hydroxyacid dehydrogenase in chromosome 9q". Biochem. Biophys. Res. Commun. 268 (2): 298–301. doi:10.1006/bbrc.2000.2122. PMID 10679197.

This article on a gene on human chromosome 9 is a stub. You can help Wikipedia by adding missing information.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000137106 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000035637 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid10524214-5] Rumsby G, Cregeen DP (Nov 1999). "Identification and expression of a cDNA for human hydroxypyruvate/glyoxylate reductase". Biochim Biophys Acta. 1446 (3): 383–8. doi:10.1016/S0167-4781(99)00105-0. PMID 10524214.

[pmid10484776-6] Cramer SD, Ferree PM, Lin K, Milliner DS, Holmes RP (Dec 1999). "The gene encoding hydroxypyruvate reductase (GRHPR) is mutated in patients with primary hyperoxaluria type II". Hum Mol Genet. 8 (11): 2063–9. doi:10.1093/hmg/8.11.2063. PMID 10484776.

[entrez-7] 1 2 "Entrez Gene: GRHPR glyoxylate reductase/hydroxypyruvate reductase".

[pmid18982322-8] Takaoka N, Takayama T, Miyazaki M, Nagata M, Ozono S (Dec 2008). "Modification of primers for GRHPR genotyping: avoiding allele dropout by single nucleotide polymorphisms and homology sequence". Urol Res. 36 (6): 297–302. doi:10.1007/s00240-008-0159-z. PMID 18982322. S2CID 12234158.

v t e Oxidoreductases: alcohol oxidoreductases (EC 1.1)
1.1.1: NAD/NADP acceptor	3-hydroxyacyl-CoA dehydrogenase 3-hydroxybutyryl-CoA dehydrogenase 6-Phosphogluconate dehydrogenase Alcohol dehydrogenase Aldo-keto reductase 1A1 1B1 1B10 1C1 1C3 1C4 7A2 Aldose reductase Beta-Ketoacyl ACP reductase Carbohydrate dehydrogenases Carnitine dehydrogenase D-malate dehydrogenase (decarboxylating) DXP reductoisomerase Glucose-6-phosphate dehydrogenase Glycerol-3-phosphate dehydrogenase HMG-CoA reductase IMP dehydrogenase Isocitrate dehydrogenase Lactate dehydrogenase L-threonine dehydrogenase L-xylulose reductase Malate dehydrogenase Malate dehydrogenase (decarboxylating) Malate dehydrogenase (NADP+) Malate dehydrogenase (oxaloacetate-decarboxylating) Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) Sorbitol dehydrogenase Hydroxysteroid dehydrogenase: 3β 3β-HSD NSDHL 11β 11β-HSD1 11β-HSD2 17β
1.1.2: cytochrome acceptor	D-lactate dehydrogenase (cytochrome) D-lactate dehydrogenase (cytochrome c-553) Mannitol dehydrogenase (cytochrome)
1.1.3: oxygen acceptor	Alcohol oxidase Glucose oxidase L-gulonolactone oxidase L-lactate oxidase Xanthine oxidase
1.1.4: disulfide as acceptor	Vitamin K epoxide reductase Vitamin-K-epoxide reductase (warfarin-insensitive)
1.1.5: quinone/similar acceptor	Malate dehydrogenase (quinone) Quinoprotein glucose dehydrogenase
1.1.99: other acceptors	Choline dehydrogenase L2HGDH

GRHPR

References

External links

Further reading