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IDH3A

January 26, 2023

Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial (IDH3α) is an enzyme that in humans is encoded by the IDH3A gene.[5][6]

IDH3A
Identifiers
AliasesIDH3A, isocitrate dehydrogenase 3 (NAD(+)) alpha, isocitrate dehydrogenase (NAD(+)) 3 alpha, isocitrate dehydrogenase (NAD(+)) 3 catalytic subunit alpha, RP90
External IDsOMIM: 601149 MGI: 1915084 HomoloGene: 4037 GeneCards: IDH3A
Orthologs
SpeciesHumanMouse
Entrez

3419

67834

Ensembl

ENSG00000166411

ENSMUSG00000032279

UniProt

P50213

Q9D6R2

RefSeq (mRNA)

NM_005530

NM_029573

RefSeq (protein)

NP_005521

NP_083849

Location (UCSC)Chr 15: 78.13 – 78.17 MbChr 9: 54.49 – 54.51 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Isocitrate dehydrogenases (IDHs) catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. These enzymes belong to two distinct subclasses, one of which utilizes NAD(+) as the electron acceptor and the other NADP(+). Five isocitrate dehydrogenases have been reported: three NAD(+)-dependent isocitrate dehydrogenases, which localize to the mitochondrial matrix, and two NADP(+)-dependent isocitrate dehydrogenases, one of which is mitochondrial and the other predominantly cytosolic. NAD(+)-dependent isocitrate dehydrogenases catalyze the allosterically regulated rate-limiting step of the tricarboxylic acid cycle. Each isozyme is a heterotetramer that is composed of two alpha subunits, one beta subunit, and one gamma subunit. The protein encoded by this gene is the alpha subunit of one isozyme of NAD(+)-dependent isocitrate dehydrogenase. [provided by RefSeq, Jul 2008][6]

Structure

IDH3 is one of three isocitrate dehydrogenase isozymes, the other two being IDH1 and IDH2, and encoded by one of five isocitrate dehydrogenase genes, which are IDH1, IDH2, IDH3A, IDH3B, and IDH3G.[7] The genes IDH3A, IDH3B, and IDH3G encode subunits of IDH3, which is a heterotetramer composed of two 37-kDa α subunits (IDH3α), one 39-kDa β subunit (IDH3β), and one 39-kDa γ subunit (IDH3γ), each with distinct isoelectric points.[8][9][10] Alignment of their amino acid sequences reveals ~40% identity between IDH3α and IDH3β, ~42% identity between IDH3α and IDH3γ, and an even closer identity of 53% between IDH3β and IDH3γ, for an overall 34% identity and 23% similarity across all three subunit types.[9][10][11][12] Notably, Arg88 in IDH3α is essential for IDH3 catalytic activity, whereas the equivalent Arg99 in IDH3β and Arg97 in IDH3γ are largely involved in the enzyme’s allosteric regulation by ADP and NAD.[11] Thus, it is possible that these subunits arose from gene duplication of a common ancestral gene, and the original catalytic Arg residue were adapted to allosteric functions in the β- and γ-subunits.[9][11] Likewise, Asp181 in IDH3α is essential for catalysis, while the equivalent Asp192 in IDH3β and Asp190 in IDH3γ enhance NAD- and Mn2+-binding.[9] Since the oxidative decarboxylation catalyzed by IDH3 requires binding of NAD, Mn2+, and the substrate isocitrate, all three subunits participate in the catalytic reaction.[10][11] Moreover, studies of the enzyme in pig heart reveal that the αβ and αγ dimers constitute two binding sites for each of its ligands, including isocitrate, Mn2+, and NAD, in one IDH3 tetramer.[9][10]

Function

As an isocitrate dehydrogenase, IDH3 catalyzes the irreversible oxidative decarboxylation of isocitrate to yield α-ketoglutarate (α-KG) and CO2 as part of the TCA cycle in glucose metabolism.[5][8][9][10][11] This step also allows for the concomitant reduction of NAD+ to NADH, which is then used to generate ATP through the electron transport chain. Notably, IDH3 relies on NAD+ as its electron acceptor, as opposed to NADP+ like IDH1 and IDH2.[8][9] IDH3 activity is regulated by the energy needs of the cell: when the cell requires energy, IDH3 is activated by ADP; and when energy is no longer required, IDH3 is inhibited by ATP and NADH.[9][10] This allosteric regulation allows IDH3 to function as a rate-limiting step in the TCA cycle.[5][13] Within cells, IDH3 and its subunits have been observed to localize to the mitochondria.[5][9][10]

Clinical significance

IDH3α expression has been linked to cancer, with high basal expression in multiple cancer cell lines and increased expression indicative of poorer prognosis in cancer patients. IDH3α is proposed to promote tumor growth as a regulator of α-KG, which subsequently regulates HIF-1. HIF-1 is largely known for shifting glucose metabolism from oxidative phosphorylation to aerobic glycolysis in cancer cells (the Warburg effect). Moreover, IDH3α activity leads to angiogenesis and metabolic reprogramming to provide the necessary nutrients for continuous cell growth. Meanwhile, silencing IDH3α is observed to obstruct tumor growth. Thus, IDH3α may prove to be a promising therapeutic target in treating cancer.[8]

IDH3α is also implicated in psychiatric disorders. In particular, IDH3α expression in the cerebellum is observed to be significantly lower for bipolar disorder, major depressive disorder, and schizophrenia. The abnormal IDH3α levels may disrupt mitochondrial function and contribute to the pathogenesis of these disorders.[13]

Mutations in this gene have been associated with autosomal recessive retinitis pigmentosa.[14]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000166411 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000032279 - 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.
  5. ^ a b c d Huh TL, Kim YO, Oh IU, Song BJ, Inazawa J (March 1996). "Assignment of the human mitochondrial NAD+ -specific isocitrate dehydrogenase alpha subunit (IDH3A) gene to 15q25.1-->q25.2by in situ hybridization". Genomics. 32 (2): 295–6. doi:10.1006/geno.1996.0120. PMID 8833160.
  6. ^ a b "Entrez Gene: IDH3A isocitrate dehydrogenase 3 (NAD+) alpha".
  7. ^ Dimitrov L, Hong CS, Yang C, Zhuang Z, Heiss JD (2015). "New developments in the pathogenesis and therapeutic targeting of the IDH1 mutation in glioma". International Journal of Medical Sciences. 12 (3): 201–13. doi:10.7150/ijms.11047. PMC 4323358. PMID 25678837.
  8. ^ a b c d Zeng L, Morinibu A, Kobayashi M, Zhu Y, Wang X, Goto Y, Yeom CJ, Zhao T, Hirota K, Shinomiya K, Itasaka S, Yoshimura M, Guo G, Hammond EM, Hiraoka M, Harada H (September 2015). "Aberrant IDH3α expression promotes malignant tumor growth by inducing HIF-1-mediated metabolic reprogramming and angiogenesis". Oncogene. 34 (36): 4758–66. doi:10.1038/onc.2014.411. PMID 25531325.
  9. ^ a b c d e f g h i Bzymek KP, Colman RF (May 2007). "Role of alpha-Asp181, beta-Asp192, and gamma-Asp190 in the distinctive subunits of human NAD-specific isocitrate dehydrogenase". Biochemistry. 46 (18): 5391–7. doi:10.1021/bi700061t. PMID 17432878.
  10. ^ a b c d e f g Soundar S, O'hagan M, Fomulu KS, Colman RF (July 2006). "Identification of Mn2+-binding aspartates from alpha, beta, and gamma subunits of human NAD-dependent isocitrate dehydrogenase". The Journal of Biological Chemistry. 281 (30): 21073–81. doi:10.1074/jbc.m602956200. PMID 16737955.
  11. ^ a b c d e Soundar S, Park JH, Huh TL, Colman RF (December 2003). "Evaluation by mutagenesis of the importance of 3 arginines in alpha, beta, and gamma subunits of human NAD-dependent isocitrate dehydrogenase". The Journal of Biological Chemistry. 278 (52): 52146–53. doi:10.1074/jbc.m306178200. PMID 14555658.
  12. ^ Dange M, Colman RF (July 2010). "Each conserved active site tyr in the three subunits of human isocitrate dehydrogenase has a different function". The Journal of Biological Chemistry. 285 (27): 20520–5. doi:10.1074/jbc.m110.115386. PMC 2898308. PMID 20435888.
  13. ^ a b Yoshimi N, Futamura T, Bergen SE, Iwayama Y, Ishima T, Sellgren C, Ekman CJ, Jakobsson J, Pålsson E, Kakumoto K, Ohgi Y, Yoshikawa T, Landén M, Hashimoto K (November 2016). "Cerebrospinal fluid metabolomics identifies a key role of isocitrate dehydrogenase in bipolar disorder: evidence in support of mitochondrial dysfunction hypothesis". Molecular Psychiatry. 21 (11): 1504–1510. doi:10.1038/mp.2015.217. PMC 5078854. PMID 26782057.
  14. ^ Peter VG, Nikopoulos K, Quinodoz M, Granse L, Farinelli P, Superti-Furga A, Andréasson S, Rivolta C (April 2019). "A novel missense variant in IDH3A causes autosomal recessive retinitis pigmentosa". Ophthalmic Genetics. 40 (2): 177–181. doi:10.1080/13816810.2019.1605391. PMID 31012789. S2CID 128362107.

Further reading

  • Anderson NL, Anderson NG (November 2002). "The human plasma proteome: history, character, and diagnostic prospects". Molecular & Cellular Proteomics. 1 (11): 845–67. doi:10.1074/mcp.R200007-MCP200. PMID 12488461.
  • Kim YO, Oh IU, Park HS, Jeng J, Song BJ, Huh TL (May 1995). "Characterization of a cDNA clone for human NAD(+)-specific isocitrate dehydrogenase alpha-subunit and structural comparison with its isoenzymes from different species". The Biochemical Journal. 308 (Pt 1): 63–8. doi:10.1042/bj3080063. PMC 1136843. PMID 7755589.
  • Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Kim YO, Koh HJ, Kim SH, Jo SH, Huh JW, Jeong KS, Lee IJ, Song BJ, Huh TL (December 1999). "Identification and functional characterization of a novel, tissue-specific NAD(+)-dependent isocitrate dehydrogenase beta subunit isoform". The Journal of Biological Chemistry. 274 (52): 36866–75. doi:10.1074/jbc.274.52.36866. PMID 10601238.
  • Weiss C, Zeng Y, Huang J, Sobocka MB, Rushbrook JI (February 2000). "Bovine NAD+-dependent isocitrate dehydrogenase: alternative splicing and tissue-dependent expression of subunit 1". Biochemistry. 39 (7): 1807–16. doi:10.1021/bi991691i. PMID 10677231.
  • Adkins JN, Varnum SM, Auberry KJ, Moore RJ, Angell NH, Smith RD, Springer DL, Pounds JG (December 2002). "Toward a human blood serum proteome: analysis by multidimensional separation coupled with mass spectrometry". Molecular & Cellular Proteomics. 1 (12): 947–55. doi:10.1074/mcp.M200066-MCP200. PMID 12543931.
  • Soundar S, Park JH, Huh TL, Colman RF (December 2003). "Evaluation by mutagenesis of the importance of 3 arginines in alpha, beta, and gamma subunits of human NAD-dependent isocitrate dehydrogenase". The Journal of Biological Chemistry. 278 (52): 52146–53. doi:10.1074/jbc.M306178200. PMID 14555658.
  • Guo D, Han J, Adam BL, Colburn NH, Wang MH, Dong Z, Eizirik DL, She JX, Wang CY (December 2005). "Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress". Biochemical and Biophysical Research Communications. 337 (4): 1308–18. doi:10.1016/j.bbrc.2005.09.191. PMID 16236267.
  • Soundar S, O'hagan M, Fomulu KS, Colman RF (July 2006). "Identification of Mn2+-binding aspartates from alpha, beta, and gamma subunits of human NAD-dependent isocitrate dehydrogenase". The Journal of Biological Chemistry. 281 (30): 21073–81. doi:10.1074/jbc.M602956200. PMID 16737955.
  • Bzymek KP, Colman RF (May 2007). "Role of alpha-Asp181, beta-Asp192, and gamma-Asp190 in the distinctive subunits of human NAD-specific isocitrate dehydrogenase". Biochemistry. 46 (18): 5391–7. doi:10.1021/bi700061t. PMID 17432878.

January 26, 2023
idh3a, isocitrate, dehydrogenase, subunit, alpha, mitochondrial, idh3α, enzyme, that, humans, encoded, gene, identifiersaliases, isocitrate, dehydrogenase, alpha, isocitrate, dehydrogenase, alpha, isocitrate, dehydrogenase, catalytic, subunit, alpha, rp90exter. Isocitrate dehydrogenase NAD subunit alpha mitochondrial IDH3a is an enzyme that in humans is encoded by the IDH3A gene 5 6 IDH3AIdentifiersAliasesIDH3A isocitrate dehydrogenase 3 NAD alpha isocitrate dehydrogenase NAD 3 alpha isocitrate dehydrogenase NAD 3 catalytic subunit alpha RP90External IDsOMIM 601149 MGI 1915084 HomoloGene 4037 GeneCards IDH3AGene location Human Chr Chromosome 15 human 1 Band15q25 1Start78 131 498 bp 1 End78 171 945 bp 1 Gene location Mouse Chr Chromosome 9 mouse 2 Band9 9 A5 3Start54 493 618 bp 2 End54 511 945 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inright ventricleleft ventriclerectumprefrontal cortexgastrocnemius musclebiceps brachiinucleus accumbensBrodmann area 9Left adrenal glandtransverse colonTop expressed insternocleidomastoid muscletriceps brachii muscletemporal muscledigastric musclevastus lateralis muscleright ventricleatrioventricular valveintercostal musclebrown adipose tissueatriumMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionoxidoreductase activity acting on the CH OH group of donors NAD or NADP as acceptor oxidoreductase activity NAD binding metal ion binding magnesium ion binding isocitrate dehydrogenase NAD activityCellular componentmyelin sheath mitochondrial matrix mitochondrion nucleusBiological processtricarboxylic acid cycle carbohydrate metabolic process isocitrate metabolic processSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez341967834EnsemblENSG00000166411ENSMUSG00000032279UniProtP50213Q9D6R2RefSeq mRNA NM 005530NM 029573RefSeq protein NP 005521NP 083849Location UCSC Chr 15 78 13 78 17 MbChr 9 54 49 54 51 MbPubMed search 3 4 WikidataView Edit HumanView Edit MouseIsocitrate dehydrogenases IDHs catalyze the oxidative decarboxylation of isocitrate to 2 oxoglutarate These enzymes belong to two distinct subclasses one of which utilizes NAD as the electron acceptor and the other NADP Five isocitrate dehydrogenases have been reported three NAD dependent isocitrate dehydrogenases which localize to the mitochondrial matrix and two NADP dependent isocitrate dehydrogenases one of which is mitochondrial and the other predominantly cytosolic NAD dependent isocitrate dehydrogenases catalyze the allosterically regulated rate limiting step of the tricarboxylic acid cycle Each isozyme is a heterotetramer that is composed of two alpha subunits one beta subunit and one gamma subunit The protein encoded by this gene is the alpha subunit of one isozyme of NAD dependent isocitrate dehydrogenase provided by RefSeq Jul 2008 6 Contents 1 Structure 2 Function 3 Clinical significance 4 See also 5 References 6 Further readingStructure EditIDH3 is one of three isocitrate dehydrogenase isozymes the other two being IDH1 and IDH2 and encoded by one of five isocitrate dehydrogenase genes which are IDH1 IDH2 IDH3A IDH3B and IDH3G 7 The genes IDH3A IDH3B and IDH3G encode subunits of IDH3 which is a heterotetramer composed of two 37 kDa a subunits IDH3a one 39 kDa b subunit IDH3b and one 39 kDa g subunit IDH3g each with distinct isoelectric points 8 9 10 Alignment of their amino acid sequences reveals 40 identity between IDH3a and IDH3b 42 identity between IDH3a and IDH3g and an even closer identity of 53 between IDH3b and IDH3g for an overall 34 identity and 23 similarity across all three subunit types 9 10 11 12 Notably Arg88 in IDH3a is essential for IDH3 catalytic activity whereas the equivalent Arg99 in IDH3b and Arg97 in IDH3g are largely involved in the enzyme s allosteric regulation by ADP and NAD 11 Thus it is possible that these subunits arose from gene duplication of a common ancestral gene and the original catalytic Arg residue were adapted to allosteric functions in the b and g subunits 9 11 Likewise Asp181 in IDH3a is essential for catalysis while the equivalent Asp192 in IDH3b and Asp190 in IDH3g enhance NAD and Mn2 binding 9 Since the oxidative decarboxylation catalyzed by IDH3 requires binding of NAD Mn2 and the substrate isocitrate all three subunits participate in the catalytic reaction 10 11 Moreover studies of the enzyme in pig heart reveal that the ab and ag dimers constitute two binding sites for each of its ligands including isocitrate Mn2 and NAD in one IDH3 tetramer 9 10 Function EditAs an isocitrate dehydrogenase IDH3 catalyzes the irreversible oxidative decarboxylation of isocitrate to yield a ketoglutarate a KG and CO2 as part of the TCA cycle in glucose metabolism 5 8 9 10 11 This step also allows for the concomitant reduction of NAD to NADH which is then used to generate ATP through the electron transport chain Notably IDH3 relies on NAD as its electron acceptor as opposed to NADP like IDH1 and IDH2 8 9 IDH3 activity is regulated by the energy needs of the cell when the cell requires energy IDH3 is activated by ADP and when energy is no longer required IDH3 is inhibited by ATP and NADH 9 10 This allosteric regulation allows IDH3 to function as a rate limiting step in the TCA cycle 5 13 Within cells IDH3 and its subunits have been observed to localize to the mitochondria 5 9 10 Clinical significance EditIDH3a expression has been linked to cancer with high basal expression in multiple cancer cell lines and increased expression indicative of poorer prognosis in cancer patients IDH3a is proposed to promote tumor growth as a regulator of a KG which subsequently regulates HIF 1 HIF 1 is largely known for shifting glucose metabolism from oxidative phosphorylation to aerobic glycolysis in cancer cells the Warburg effect Moreover IDH3a activity leads to angiogenesis and metabolic reprogramming to provide the necessary nutrients for continuous cell growth Meanwhile silencing IDH3a is observed to obstruct tumor growth Thus IDH3a may prove to be a promising therapeutic target in treating cancer 8 IDH3a is also implicated in psychiatric disorders In particular IDH3a expression in the cerebellum is observed to be significantly lower for bipolar disorder major depressive disorder and schizophrenia The abnormal IDH3a levels may disrupt mitochondrial function and contribute to the pathogenesis of these disorders 13 Mutations in this gene have been associated with autosomal recessive retinitis pigmentosa 14 See also EditIDH1 IDH2 IDH3B IDH3GReferences Edit a b c GRCh38 Ensembl release 89 ENSG00000166411 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000032279 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 c d Huh TL Kim YO Oh IU Song BJ Inazawa J March 1996 Assignment of the human mitochondrial NAD specific isocitrate dehydrogenase alpha subunit IDH3A gene to 15q25 1 gt q25 2by in situ hybridization Genomics 32 2 295 6 doi 10 1006 geno 1996 0120 PMID 8833160 a b Entrez Gene IDH3A isocitrate dehydrogenase 3 NAD alpha Dimitrov L Hong CS Yang C Zhuang Z Heiss JD 2015 New developments in the pathogenesis and therapeutic targeting of the IDH1 mutation in glioma International Journal of Medical Sciences 12 3 201 13 doi 10 7150 ijms 11047 PMC 4323358 PMID 25678837 a b c d Zeng L Morinibu A Kobayashi M Zhu Y Wang X Goto Y Yeom CJ Zhao T Hirota K Shinomiya K Itasaka S Yoshimura M Guo G Hammond EM Hiraoka M Harada H September 2015 Aberrant IDH3a expression promotes malignant tumor growth by inducing HIF 1 mediated metabolic reprogramming and angiogenesis Oncogene 34 36 4758 66 doi 10 1038 onc 2014 411 PMID 25531325 a b c d e f g h i Bzymek KP Colman RF May 2007 Role of alpha Asp181 beta Asp192 and gamma Asp190 in the distinctive subunits of human NAD specific isocitrate dehydrogenase Biochemistry 46 18 5391 7 doi 10 1021 bi700061t PMID 17432878 a b c d e f g Soundar S O hagan M Fomulu KS Colman RF July 2006 Identification of Mn2 binding aspartates from alpha beta and gamma subunits of human NAD dependent isocitrate dehydrogenase The Journal of Biological Chemistry 281 30 21073 81 doi 10 1074 jbc m602956200 PMID 16737955 a b c d e Soundar S Park JH Huh TL Colman RF December 2003 Evaluation by mutagenesis of the importance of 3 arginines in alpha beta and gamma subunits of human NAD dependent isocitrate dehydrogenase The Journal of Biological Chemistry 278 52 52146 53 doi 10 1074 jbc m306178200 PMID 14555658 Dange M Colman RF July 2010 Each conserved active site tyr in the three subunits of human isocitrate dehydrogenase has a different function The Journal of Biological Chemistry 285 27 20520 5 doi 10 1074 jbc m110 115386 PMC 2898308 PMID 20435888 a b Yoshimi N Futamura T Bergen SE Iwayama Y Ishima T Sellgren C Ekman CJ Jakobsson J Palsson E Kakumoto K Ohgi Y Yoshikawa T Landen M Hashimoto K November 2016 Cerebrospinal fluid metabolomics identifies a key role of isocitrate dehydrogenase in bipolar disorder evidence in support of mitochondrial dysfunction hypothesis Molecular Psychiatry 21 11 1504 1510 doi 10 1038 mp 2015 217 PMC 5078854 PMID 26782057 Peter VG Nikopoulos K Quinodoz M Granse L Farinelli P Superti Furga A Andreasson S Rivolta C April 2019 A novel missense variant in IDH3A causes autosomal recessive retinitis pigmentosa Ophthalmic Genetics 40 2 177 181 doi 10 1080 13816810 2019 1605391 PMID 31012789 S2CID 128362107 Further reading EditAnderson NL Anderson NG November 2002 The human plasma proteome history character and diagnostic prospects Molecular amp Cellular Proteomics 1 11 845 67 doi 10 1074 mcp R200007 MCP200 PMID 12488461 Kim YO Oh IU Park HS Jeng J Song BJ Huh TL May 1995 Characterization of a cDNA clone for human NAD specific isocitrate dehydrogenase alpha subunit and structural comparison with its isoenzymes from different species The Biochemical Journal 308 Pt 1 63 8 doi 10 1042 bj3080063 PMC 1136843 PMID 7755589 Maruyama K Sugano S January 1994 Oligo capping a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides Gene 138 1 2 171 4 doi 10 1016 0378 1119 94 90802 8 PMID 8125298 Suzuki Y Yoshitomo Nakagawa K Maruyama K Suyama A Sugano S October 1997 Construction and characterization of a full length enriched and a 5 end enriched cDNA library Gene 200 1 2 149 56 doi 10 1016 S0378 1119 97 00411 3 PMID 9373149 Kim YO Koh HJ Kim SH Jo SH Huh JW Jeong KS Lee IJ Song BJ Huh TL December 1999 Identification and functional characterization of a novel tissue specific NAD dependent isocitrate dehydrogenase beta subunit isoform The Journal of Biological Chemistry 274 52 36866 75 doi 10 1074 jbc 274 52 36866 PMID 10601238 Weiss C Zeng Y Huang J Sobocka MB Rushbrook JI February 2000 Bovine NAD dependent isocitrate dehydrogenase alternative splicing and tissue dependent expression of subunit 1 Biochemistry 39 7 1807 16 doi 10 1021 bi991691i PMID 10677231 Adkins JN Varnum SM Auberry KJ Moore RJ Angell NH Smith RD Springer DL Pounds JG December 2002 Toward a human blood serum proteome analysis by multidimensional separation coupled with mass spectrometry Molecular amp Cellular Proteomics 1 12 947 55 doi 10 1074 mcp M200066 MCP200 PMID 12543931 Soundar S Park JH Huh TL Colman RF December 2003 Evaluation by mutagenesis of the importance of 3 arginines in alpha beta and gamma subunits of human NAD dependent isocitrate dehydrogenase The Journal of Biological Chemistry 278 52 52146 53 doi 10 1074 jbc M306178200 PMID 14555658 Guo D Han J Adam BL Colburn NH Wang MH Dong Z Eizirik DL She JX Wang CY December 2005 Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation induced stress Biochemical and Biophysical Research Communications 337 4 1308 18 doi 10 1016 j bbrc 2005 09 191 PMID 16236267 Soundar S O hagan M Fomulu KS Colman RF July 2006 Identification of Mn2 binding aspartates from alpha beta and gamma subunits of human NAD dependent isocitrate dehydrogenase The Journal of Biological Chemistry 281 30 21073 81 doi 10 1074 jbc M602956200 PMID 16737955 Bzymek KP Colman RF May 2007 Role of alpha Asp181 beta Asp192 and gamma Asp190 in the distinctive subunits of human NAD specific isocitrate dehydrogenase Biochemistry 46 18 5391 7 doi 10 1021 bi700061t PMID 17432878 Portal Biology Retrieved from https en wikipedia org w index php title IDH3A amp oldid 1112354650, wikipedia, wiki, book, books, library,

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