GRHPR: Difference between revisions

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Latest revision as of 09:05, 31 August 2017

Glyoxylate reductase/hydroxypyruvate reductase is an enzyme that in humans is encoded by the GRHPR gene.^[1]^[2]^[3]

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.^[3] GRHPR mutation analysis needs to pay attention to primer design, because allele dropout can cause false-positive result.^[4]

References

↑ 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.
↑ ^3.0 ^3.1 "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.

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. 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.
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 expanding it.

[pmid10524214-1] 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.

[pmid10484776-2] 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-3] 3.0 ^3.1 "Entrez Gene: GRHPR glyoxylate reductase/hydroxypyruvate reductase".

[pmid18982322-4] 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.

[1]

[2]

[3]

[4]

@@ Line 1: / Line 1: @@
+{{Infobox_gene}}
+'''Glyoxylate reductase/hydroxypyruvate reductase''' is an [[enzyme]] that in humans is encoded by the ''GRHPR'' [[gene]].<ref name="pmid10524214">{{cite journal |vauthors=Rumsby G, Cregeen DP | title = Identification and expression of a cDNA for human hydroxypyruvate/glyoxylate reductase | journal = Biochim Biophys Acta | volume = 1446 | issue = 3 | pages = 383–8 |date=Nov 1999 | pmid = 10524214 | pmc =  | doi =  10.1016/S0167-4781(99)00105-0}}</ref><ref name="pmid10484776">{{cite journal |vauthors=Cramer SD, Ferree PM, Lin K, Milliner DS, Holmes RP | title = The gene encoding hydroxypyruvate reductase (GRHPR) is mutated in patients with primary hyperoxaluria type II | journal = Hum Mol Genet | volume = 8 | issue = 11 | pages = 2063–9 |date=Dec 1999 | pmid = 10484776 | pmc =  | doi =10.1093/hmg/8.11.2063  }}</ref><ref name="entrez"/>
+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.<ref name="entrez">{{cite web | title = Entrez Gene: GRHPR glyoxylate reductase/hydroxypyruvate reductase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9380| accessdate = }}</ref> GRHPR mutation analysis needs to pay attention to primer design, because allele dropout can cause false-positive result.<ref name="pmid18982322">{{cite journal |vauthors=Takaoka N, Takayama T, Miyazaki M, Nagata M, Ozono S | title = Modification of primers for GRHPR genotyping: avoiding allele dropout by single nucleotide polymorphisms and homology sequence. | journal = Urol Res. | volume = 36 | issue = 6 | pages = 297–302 |date=Dec 2008 | pmid = 18982322 | pmc =  | doi = 10.1007/s00240-008-0159-z }}</ref>
+==References==
+{{Reflist}}
+==External links==
+* [https://www.ncbi.nlm.nih.gov/bookshelf/br.fcgi?book=gene&part=ph2  GeneReviews/NCBI/NIH/UW entry on Primary Hyperoxaluria Type 2]
+==Further reading==
+{{Refbegin | 2}}
+{{PBB_Further_reading
+| citations =
+*{{Cite journal   |vauthors=Takayama T, Nagata M, Ozono S, etal |title=A novel mutation in the GRHPR gene in a Japanese patient with primary hyperoxaluria type 2 |journal=Nephrol. Dial. Transplant. |volume=22 |issue= 8 |pages= 2371–4 |year= 2007 |pmid= 17510093 |doi= 10.1093/ndt/gfm271  | pmc=2413148 }}
+*{{Cite journal  |vauthors=Booth MP, Conners R, Rumsby G, Brady RL |title=Structural basis of substrate specificity in human glyoxylate reductase/hydroxypyruvate reductase |journal=J. Mol. Biol. |volume=360 |issue= 1 |pages= 178–89 |year= 2006 |pmid= 16756993 |doi= 10.1016/j.jmb.2006.05.018 }}
+*{{Cite journal   |vauthors=Mehrle A, Rosenfelder H, Schupp I, etal |title=The LIFEdb database in 2006 |journal=Nucleic Acids Res. |volume=34 |issue= Database issue |pages= D415–8 |year= 2006 |pmid= 16381901 |doi= 10.1093/nar/gkj139  | pmc=1347501 }}
+*{{Cite journal   |vauthors=Wiemann S, Arlt D, Huber W, etal |title=From ORFeome to Biology: A Functional Genomics Pipeline |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136–44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704  | pmc=528930 }}
+*{{Cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 }}
+*{{Cite journal  |vauthors=Lehner B, Sanderson CM |title=A Protein Interaction Framework for Human mRNA Degradation |journal=Genome Res. |volume=14 |issue= 7 |pages= 1315–23 |year= 2004 |pmid= 15231747 |doi= 10.1101/gr.2122004  | pmc=442147 }}
+*{{Cite journal   |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
+*{{Cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 }}
+*{{Cite journal   |vauthors=Simpson JC, Wellenreuther R, Poustka A, etal |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287–92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058  | pmc=1083732 }}
+*{{Cite journal  |vauthors=Hartley JL, Temple GF, Brasch MA |title=DNA Cloning Using In Vitro Site-Specific Recombination |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788–95 |year= 2001 |pmid= 11076863 |doi=10.1101/gr.143000  | pmc=310948  }}
+*{{Cite journal  |vauthors=Webster KE, Ferree PM, Holmes RP, Cramer SD |title=Identification of missense, nonsense, and deletion mutations in the GRHPR gene in patients with primary hyperoxaluria type II (PH2) |journal=Hum. Genet. |volume=107 |issue= 2 |pages= 176–85 |year= 2000 |pmid= 11030416 |doi=10.1007/s004390000351  }}
+*{{Cite journal   |vauthors=Huang T, Yang W, Pereira AC, etal |title=Cloning and characterization of a putative human d-2-hydroxyacid dehydrogenase in chromosome 9q |journal=Biochem. Biophys. Res. Commun. |volume=268 |issue= 2 |pages= 298–301 |year= 2000 |pmid= 10679197 |doi= 10.1006/bbrc.2000.2122 }}
+}}
+{{Refend}}
+{{PDB Gallery|geneid=9380}}
 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
 {{PBB_Controls
 | update_page = yes
 | require_manual_inspection = no
 | update_protein_box = yes
-| update_summary = yes
+| update_summary = no
 | update_citations = yes
 }}
-<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
+{{Alcohol oxidoreductases}}
-{{GNF_Protein_box
- | image = PBB_Protein_GRHPR_image.jpg
- | image_source = [[Protein_Data_Bank|PDB]] rendering based on 2gcg.
- | PDB = {{PDB2|2gcg}}, {{PDB2|2h1s}}
- | Name = Glyoxylate reductase/hydroxypyruvate reductase
- | HGNCid = 4570
- | Symbol = GRHPR
- | AltSymbols =; PH2; GLXR
- | OMIM = 604296
- | ECnumber =
- | Homologene = 49088
- | MGIid = 1923488
- | GeneAtlas_image1 = PBB_GE_GRHPR_214864_s_at_tn.png
- | GeneAtlas_image2 = PBB_GE_GRHPR_201347_x_at_tn.png
- | GeneAtlas_image3 = PBB_GE_GRHPR_216308_x_at_tn.png
- | Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008465 |text = glycerate dehydrogenase activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0016616 |text = oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor}} {{GNF_GO|id=GO:0016618 |text = hydroxypyruvate reductase activity}} {{GNF_GO|id=GO:0030267 |text = glyoxylate reductase (NADP) activity}} {{GNF_GO|id=GO:0051287 |text = NAD binding}}
- | Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
- | Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006564 |text = L-serine biosynthetic process}} {{GNF_GO|id=GO:0007588 |text = excretion}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 9380
-    | Hs_Ensembl = ENSG00000137106
-    | Hs_RefseqProtein = NP_036335
-    | Hs_RefseqmRNA = NM_012203
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = 9
-    | Hs_GenLoc_start = 37412663
-    | Hs_GenLoc_end = 37426987
-    | Hs_Uniprot = Q9UBQ7
-    | Mm_EntrezGene = 76238
-    | Mm_Ensembl = ENSMUSG00000035637
-    | Mm_RefseqmRNA = NM_080289
-    | Mm_RefseqProtein = NP_525028
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr = 4
-    | Mm_GenLoc_start = 45002504
-    | Mm_GenLoc_end = 45011797
-    | Mm_Uniprot = Q3T9Z2
-  }}
-}}
-'''Glyoxylate reductase/hydroxypyruvate reductase''', also known as '''GRHPR''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GRHPR glyoxylate reductase/hydroxypyruvate reductase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9380| accessdate = }}</ref>
-<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
-{{PBB_Summary
-| section_title =
-| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: GRHPR glyoxylate reductase/hydroxypyruvate reductase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9380| accessdate = }}</ref>
-}}
-==References==
-{{reflist|2}}
-==Further reading==
-{{refbegin | 2}}
-{{PBB_Further_reading
-| citations =
-*{{cite journal  | author=Takayama T, Nagata M, Ozono S, ''et al.'' |title=A novel mutation in the GRHPR gene in a Japanese patient with primary hyperoxaluria type 2. |journal=Nephrol. Dial. Transplant. |volume=22 |issue= 8 |pages= 2371-4 |year= 2007 |pmid= 17510093 |doi= 10.1093/ndt/gfm271 }}
-*{{cite journal  | author=Booth MP, Conners R, Rumsby G, Brady RL |title=Structural basis of substrate specificity in human glyoxylate reductase/hydroxypyruvate reductase. |journal=J. Mol. Biol. |volume=360 |issue= 1 |pages= 178-89 |year= 2006 |pmid= 16756993 |doi= 10.1016/j.jmb.2006.05.018 }}
-*{{cite journal  | author=Mehrle A, Rosenfelder H, Schupp I, ''et al.'' |title=The LIFEdb database in 2006. |journal=Nucleic Acids Res. |volume=34 |issue= Database issue |pages= D415-8 |year= 2006 |pmid= 16381901 |doi= 10.1093/nar/gkj139 }}
-*{{cite journal  | author=Wiemann S, Arlt D, Huber W, ''et al.'' |title=From ORFeome to biology: a functional genomics pipeline. |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136-44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 }}
-*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
-*{{cite journal  | author=Lehner B, Sanderson CM |title=A protein interaction framework for human mRNA degradation. |journal=Genome Res. |volume=14 |issue= 7 |pages= 1315-23 |year= 2004 |pmid= 15231747 |doi= 10.1101/gr.2122004 }}
-*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
-*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
-*{{cite journal  | author=Simpson JC, Wellenreuther R, Poustka A, ''et al.'' |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287-92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 }}
-*{{cite journal  | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi=  }}
-*{{cite journal  | author=Webster KE, Ferree PM, Holmes RP, Cramer SD |title=Identification of missense, nonsense, and deletion mutations in the GRHPR gene in patients with primary hyperoxaluria type II (PH2). |journal=Hum. Genet. |volume=107 |issue= 2 |pages= 176-85 |year= 2000 |pmid= 11030416 |doi=  }}
-*{{cite journal  | author=Huang T, Yang W, Pereira AC, ''et al.'' |title=Cloning and characterization of a putative human d-2-hydroxyacid dehydrogenase in chromosome 9q. |journal=Biochem. Biophys. Res. Commun. |volume=268 |issue= 2 |pages= 298-301 |year= 2000 |pmid= 10679197 |doi= 10.1006/bbrc.2000.2122 }}
-*{{cite journal  | author=Rumsby G, Cregeen DP |title=Identification and expression of a cDNA for human hydroxypyruvate/glyoxylate reductase. |journal=Biochim. Biophys. Acta |volume=1446 |issue= 3 |pages= 383-8 |year= 1999 |pmid= 10524214 |doi=  }}
-*{{cite journal  | author=Cramer SD, Ferree PM, Lin K, ''et al.'' |title=The gene encoding hydroxypyruvate reductase (GRHPR) is mutated in patients with primary hyperoxaluria type II. |journal=Hum. Mol. Genet. |volume=8 |issue= 11 |pages= 2063-9 |year= 1999 |pmid= 10484776 |doi=  }}
-}}
-{{refend}}
-{{protein-stub}}
+{{gene-9-stub}}
-{{WikiDoc Sources}}

v t e Oxidoreductases: alcohol oxidoreductases (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
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: Difference between revisions

Latest revision as of 09:05, 31 August 2017

References

External links

Further reading

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