GRHPR

GRHPR
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	2GCG, 2H1S, 2Q50, 2WWR
Identifikatori
Aliasi	GRHPR
Vanjski ID-jevi	OMIM: 604296 MGI: 1923488 HomoloGene: 49088 GeneCards: GRHPR
Lokacija gena (čovjek)
Hrom.	Hromosom 9 (čovjek)
Kraj	37,436,990 bp
Lokacija gena (miš)
Hrom.	Hromosom 4 (miš)
Kraj	44,990,734 bp
Obrazac RNK ekspresije
	; ; ; ;
	Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija	• glycerate dehydrogenase activity; • GO:0050229 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;
Ćelijska komponenta	• citoplazma; • peroxisomal matrix; • Egzosom; • citosol;
Biološki proces	• dicarboxylic acid metabolic process; • izlučivanje; • protein complex oligomerization; • metabolizam; • cellular nitrogen compound metabolic process; • glyoxylate metabolic process;
	Izvori:Amigo / QuickGO
Ortolozi
	9380
	76238
	ENSG00000137106
	ENSMUSG00000035637
	Q9UBQ7
	Q91Z53
	NM_012203
	NM_080289; NM_001312880
	NP_036335
	NP_001299809; NP_525028
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Gliokzilat-reduktaza/hidroksipiruvat-reduktaza je enzim koji je kod ljudi kodiran genom GRHPR.^[5]^[6]^[7]

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 328aminokiselina, а molekulska težina 35.668 Da.^[8]

C: Cistein

D: Asparaginska kiselina

E: Glutaminska kiselina

F: Fenilalanin

G: Glicin

H: Histidin

I: Izoleucin

K: Lizin

L: Leucin

M: Metionin

N: Asparagin

P: Prolin

Q: Glutamin

R: Arginin

S: Serin

T: Treonin

V: Valin

W: Triptofan

Y: Tirozin

10	20	30	40	50
MRPVRLMKVF	VTRRIPAEGR	VALARAADCE	VEQWDSDEPI	PAKELERGVA
GAHGLLCLLS	DHVDKRILDA	AGANLKVIST	MSVGIDHLAL	DEIKKRGIRV
GYTPDVLTDT	TAELAVSLLL	TTCRRLPEAI	EEVKNGGWTS	WKPLWLCGYG
LTQSTVGIIG	LGRIGQAIAR	RLKPFGVQRF	LYTGRQPRPE	EAAEFQAEFV
STPELAAQSD	FIVVACSLTP	ATEGLCNKDF	FQKMKETAVF	INISRGDVVN
QDDLYQALAS	GKIAAAGLDV	TSPEPLPTNH	PLLTLKNCVI	LPHIGSATHR
TRNTMSLLAA	NNLLAGLRGE	PMPSELKL

Funkcija

Ovaj gen kodira enzim s enzimskim aktivnostima koje imaju hidroksipiruvat-reduktaza, glioksilat-reduktaza i D-glicerat dehidrogenaza. Enzim ima široko rasprostranjenu tkivnu ekspresiju i ima ulogu u metabolizmu. Tip II hiperoksalurije uzrokovan je mutacijama u ovom genu.^[7] U analizi mutacija GRHPR treba obratiti pažnju na dizajn prajmera, jer ekscizija alela može uzrokovati lažno pozitivan rezultat.^[9]

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000137106 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000035637 - Ensembl, maj 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.
^ ^a ^b "Entrez Gene: GRHPR glyoxylate reductase/hydroxypyruvate reductase".
^ "UniProt, Q9UBQ7". Pristupljeno 9. 9. 2021.
^ 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.

Dopunska literatura

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. 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/s004395000351. 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.

Vanjski linkovi

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

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000137106 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000035637 - Ensembl, maj 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] "Entrez Gene: GRHPR glyoxylate reductase/hydroxypyruvate reductase".

[UniProt-8] "UniProt, Q9UBQ7". Pristupljeno 9. 9. 2021.

[pmid18982322-9] 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.

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p r u oksidoreduktaze: Alkoholne oksidoreduktaze (EC 1.1)
1.1.1: NAD/NADP acceptor	3-hydroxyacyl-CoA dehydrogenase 3-hydroxybutyryl-CoA 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 ) Phosphogluconate dehydrogenase 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	Glucose oxidase L-gulonolactone oxidase Xanthine oxidase Alcohol 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

p r u Enzimi
Teme	Aktivno mjesto Alosterna regulacija Difuzijski limitirani enzim EC broj Enzimska kataliza Inhibicija enzimskih reakcija Kinetika enzima Koenzim Kooperativnost Lineweaver–Burkov dijagram Michaelis–Mentenova kinetika Mjesto vezanja Spisak enzima
Tipovi	EC1 Oksidoreduktaze/spisak EC2 Transferaze/spisak EC3 Hidrolaze/spisak EC4 Lijaze/spisak EC5 Izomeraze/spisak EC6 Ligaze/spisak