# DLST

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Protein-coding gene in the species Homo sapiens

DLST Identifiers Aliases DLST, DLTS, dihydrolipoamide S-succinyltransferase, PGL7, KGD2 External IDs OMIM: 126063; MGI: 1926170; HomoloGene: 1456; GeneCards: DLST; OMA:DLST - orthologs Gene location (Human) Chr. Chromosome 14 (human)[1] Band 14q24.3 Start 74,881,891 bp[1] End 74,903,743 bp[1] Gene location (Mouse) Chr. Chromosome 12 (mouse)[2] Band 12|12 D1 Start 85,157,607 bp[2] End 85,181,619 bp[2] RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in apex of heart right adrenal cortex left ventricle gastrocnemius muscle left adrenal gland left adrenal cortex right auricle of heart secondary oocyte muscle of thigh skin of leg Top expressed in right ventricle muscle of thigh digastric muscle myocardium of ventricle thoracic diaphragm brown adipose tissue right kidney soleus muscle cardiac muscles sternocleidomastoid muscle More reference expression data BioGPS More reference expression data Gene ontology Molecular function transferase activity dihydrolipoyllysine-residue succinyltransferase activity acyltransferase activity protein binding Cellular component oxoglutarate dehydrogenase complex membrane myelin sheath mitochondrial matrix mitochondrion extracellular exosome nucleus Biological process tricarboxylic acid cycle lysine catabolic process generation of precursor metabolites and energy L-lysine catabolic process to acetyl-CoA via saccharopine metabolism cellular nitrogen compound metabolic process 2-oxoglutarate metabolic process succinyl-CoA metabolic process histone succinylation Sources:Amigo / QuickGO Orthologs Species Human Mouse Entrez 1743 78920 Ensembl ENSG00000119689 ENSMUSG00000004789 UniProt P36957 Q9D2G2 RefSeq (mRNA) NM_001244883 NM_001933 NM_030225 RefSeq (protein) NP_001231812 NP_001924 NP_084501 Location (UCSC) Chr 14: 74.88 – 74.9 Mb Chr 12: 85.16 – 85.18 Mb PubMed search [3] [4] Wikidata View/Edit Human View/Edit Mouse

**Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial** is an [enzyme](/source/Enzyme) that in humans is encoded by the *DLST* [gene](/source/Gene).[5][6]

## Interactive pathway map

*Click on genes, proteins and metabolites below to link to respective articles.* [§ 1]

[[File:

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TCACycle_WP78  [edit](http://www.wikipathways.org/index.php/Pathway:WP78)

1. **[^](#cite_ref-WikiPathways_7-0)** The interactive pathway map can be edited at WikiPathways: ["TCACycle_WP78"](http://www.wikipathways.org/index.php/Pathway:WP78).

## References

1. ^ [***a***](#cite_ref-refGRCh38Ensembl_1-0) [***b***](#cite_ref-refGRCh38Ensembl_1-1) [***c***](#cite_ref-refGRCh38Ensembl_1-2) [GRCh38: Ensembl release 89: ENSG00000119689](http://May2017.archive.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000119689) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. ^ [***a***](#cite_ref-refGRCm38Ensembl_2-0) [***b***](#cite_ref-refGRCm38Ensembl_2-1) [***c***](#cite_ref-refGRCm38Ensembl_2-2) [GRCm38: Ensembl release 89: ENSMUSG00000004789](http://May2017.archive.ensembl.org/Mus_musculus/Gene/Summary?db=core;g=ENSMUSG00000004789) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. **[^](#cite_ref-3)** ["Human PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=1743). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-4)** ["Mouse PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=78920). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-pmid8009371_5-0)** Ali G, Wasco W, Cai X, Szabo P, Sheu KF, Cooper AJ, Gaston SM, Gusella JF, Tanzi RE, Blass JP (Jul 1994). "Isolation, characterization, and mapping of gene encoding dihydrolipoyl succinyltransferase (E2k) of human alpha-ketoglutarate dehydrogenase complex". *Somat Cell Mol Genet*. **20** (2): 99–105. [doi](/source/Doi_(identifier)):[10.1007/BF02290679](https://doi.org/10.1007%2FBF02290679). [PMID](/source/PMID_(identifier)) [8009371](https://pubmed.ncbi.nlm.nih.gov/8009371). [S2CID](/source/S2CID_(identifier)) [43092605](https://api.semanticscholar.org/CorpusID:43092605).

1. **[^](#cite_ref-entrez_6-0)** ["Entrez Gene: DLST dihydrolipoamide S-succinyltransferase (E2 component of 2-oxo-glutarate complex)"](https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=1743).

## Further reading

- Chuang DT, Fisher CW, Lau KS, et al. (1991). "Maple syrup urine disease: domain structure, mutations and exon skipping in the dihydrolipoyl transacylase (E2) component of the branched-chain alpha-keto acid dehydrogenase complex". *Mol. Biol. Med*. **8** (1): 49–63. [PMID](/source/PMID_(identifier)) [1943690](https://pubmed.ncbi.nlm.nih.gov/1943690).

- Fregeau DR, Prindiville T, Coppel RL, et al. (1990). ["Inhibition of alpha-ketoglutarate dehydrogenase activity by a distinct population of autoantibodies recognizing dihydrolipoamide succinyltransferase in primary biliary cirrhosis"](https://doi.org/10.1002%2Fhep.1840110611). *Hepatology*. **11** (6): 975–81. [doi](/source/Doi_(identifier)):[10.1002/hep.1840110611](https://doi.org/10.1002%2Fhep.1840110611). [PMID](/source/PMID_(identifier)) [2365294](https://pubmed.ncbi.nlm.nih.gov/2365294). [S2CID](/source/S2CID_(identifier)) [83760368](https://api.semanticscholar.org/CorpusID:83760368).

- Ono K, Hakozaki M, Kimura A, Kochi H (1987). ["Purification, resolution, and reconstitution of rat liver branched-chain alpha-keto acid dehydrogenase complex"](https://doi.org/10.1093%2Foxfordjournals.jbchem.a121891). *J. Biochem*. **101** (1): 19–27. [doi](/source/Doi_(identifier)):[10.1093/oxfordjournals.jbchem.a121891](https://doi.org/10.1093%2Foxfordjournals.jbchem.a121891). [PMID](/source/PMID_(identifier)) [3571202](https://pubmed.ncbi.nlm.nih.gov/3571202).

- Kochi H, Seino H, Ono K (1986). "Inhibition of glycine oxidation by pyruvate, alpha-ketoglutarate, and branched-chain alpha-keto acids in rat liver mitochondria: presence of interaction between the glycine cleavage system and alpha-keto acid dehydrogenase complexes". *Arch. Biochem. Biophys*. **249** (2): 263–72. [doi](/source/Doi_(identifier)):[10.1016/0003-9861(86)90002-0](https://doi.org/10.1016%2F0003-9861%2886%2990002-0). [PMID](/source/PMID_(identifier)) [3753002](https://pubmed.ncbi.nlm.nih.gov/3753002).

- Nakano K, Takase C, Sakamoto T, et al. (1994). ["Isolation, characterization and structural organization of the gene and pseudogene for the dihydrolipoamide succinyltransferase component of the human 2-oxoglutarate dehydrogenase complex"](https://doi.org/10.1111%2Fj.1432-1033.1994.tb20010.x). *Eur. J. Biochem*. **224** (1): 179–89. [doi](/source/Doi_(identifier)):[10.1111/j.1432-1033.1994.tb20010.x](https://doi.org/10.1111%2Fj.1432-1033.1994.tb20010.x). [PMID](/source/PMID_(identifier)) [8076640](https://pubmed.ncbi.nlm.nih.gov/8076640).

- Nakano K, Takase C, Sakamoto T, et al. (1993). "An unspliced cDNA for human dihydrolipoamide succinyltransferase: characterization and mapping of the gene to chromosome 14q24.2-q24.3". *Biochem. Biophys. Res. Commun*. **196** (2): 527–33. [doi](/source/Doi_(identifier)):[10.1006/bbrc.1993.2282](https://doi.org/10.1006%2Fbbrc.1993.2282). [PMID](/source/PMID_(identifier)) [8240324](https://pubmed.ncbi.nlm.nih.gov/8240324).

- Nakano K, Matuda S, Sakamoto T, et al. (1994). "Human dihydrolipoamide succinyltransferase: cDNA cloning and localization on chromosome 14q24.2-q24.3". *Biochim. Biophys. Acta*. **1216** (3): 360–8. [doi](/source/Doi_(identifier)):[10.1016/0167-4781(93)90002-u](https://doi.org/10.1016%2F0167-4781%2893%2990002-u). [PMID](/source/PMID_(identifier)) [8268217](https://pubmed.ncbi.nlm.nih.gov/8268217).

- Cruts M, Backhovens H, Van Gassen G, et al. (1996). ["Mutation analysis of the chromosome 14q24.3 dihydrolipoyl succinyltransferase (DLST) gene in patients with early-onset Alzheimer disease"](https://repub.eur.nl/pub/72164). *Neurosci. Lett*. **199** (1): 73–7. [doi](/source/Doi_(identifier)):[10.1016/0304-3940(95)11982-3](https://doi.org/10.1016%2F0304-3940%2895%2911982-3). [hdl](/source/Hdl_(identifier)):[1765/72164](https://hdl.handle.net/1765%2F72164). [PMID](/source/PMID_(identifier)) [8584231](https://pubmed.ncbi.nlm.nih.gov/8584231). [S2CID](/source/S2CID_(identifier)) [7439684](https://api.semanticscholar.org/CorpusID:7439684).

- Bonaldo MF, Lennon G, Soares MB (1997). ["Normalization and subtraction: two approaches to facilitate gene discovery"](https://doi.org/10.1101%2Fgr.6.9.791). *Genome Res*. **6** (9): 791–806. [doi](/source/Doi_(identifier)):[10.1101/gr.6.9.791](https://doi.org/10.1101%2Fgr.6.9.791). [PMID](/source/PMID_(identifier)) [8889548](https://pubmed.ncbi.nlm.nih.gov/8889548).

- Matuda S, Kodama J, Goshi N, et al. (1998). "A polypeptide derived from mitochondrial dihydrolipoamide succinyltransferase is located on the plasma membrane in skeletal muscle". *Biochem. Biophys. Res. Commun*. **241** (1): 151–6. [doi](/source/Doi_(identifier)):[10.1006/bbrc.1997.7784](https://doi.org/10.1006%2Fbbrc.1997.7784). [PMID](/source/PMID_(identifier)) [9405249](https://pubmed.ncbi.nlm.nih.gov/9405249).

- McCartney RG, Rice JE, Sanderson SJ, et al. (1998). ["Subunit interactions in the mammalian alpha-ketoglutarate dehydrogenase complex. Evidence for direct association of the alpha-ketoglutarate dehydrogenase and dihydrolipoamide dehydrogenase components"](https://doi.org/10.1074%2Fjbc.273.37.24158). *J. Biol. Chem*. **273** (37): 24158–64. [doi](/source/Doi_(identifier)):[10.1074/jbc.273.37.24158](https://doi.org/10.1074%2Fjbc.273.37.24158). [PMID](/source/PMID_(identifier)) [9727038](https://pubmed.ncbi.nlm.nih.gov/9727038).

- Sheu KF, Brown AM, Haroutunian V, et al. (1999). "Modulation by DLST of the genetic risk of Alzheimer's disease in a very elderly population". *Ann. Neurol*. **45** (1): 48–53. [doi](/source/Doi_(identifier)):[10.1002/1531-8249(199901)45:1<48::AID-ART9>3.0.CO;2-V](https://doi.org/10.1002%2F1531-8249%28199901%2945%3A1%3C48%3A%3AAID-ART9%3E3.0.CO%3B2-V). [PMID](/source/PMID_(identifier)) [9894876](https://pubmed.ncbi.nlm.nih.gov/9894876). [S2CID](/source/S2CID_(identifier)) [40038247](https://api.semanticscholar.org/CorpusID:40038247).

- Ma Q, Chan P, Yang J (2002). "[Association between DLST gene polymorphism and Alzheimer's disease]". *Zhonghua Yi Xue Za Zhi*. **81** (20): 1246–8. [PMID](/source/PMID_(identifier)) [11825528](https://pubmed.ncbi.nlm.nih.gov/11825528).

- 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"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139241). *Proc. Natl. Acad. Sci. U.S.A*. **99** (26): 16899–903. [Bibcode](/source/Bibcode_(identifier)):[2002PNAS...9916899M](https://ui.adsabs.harvard.edu/abs/2002PNAS...9916899M). [doi](/source/Doi_(identifier)):[10.1073/pnas.242603899](https://doi.org/10.1073%2Fpnas.242603899). [PMC](/source/PMC_(identifier)) [139241](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139241). [PMID](/source/PMID_(identifier)) [12477932](https://pubmed.ncbi.nlm.nih.gov/12477932).

- Kanamori T, Nishimaki K, Asoh S, et al. (2003). ["Truncated product of the bifunctional DLST gene involved in biogenesis of the respiratory chain"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC162151). *EMBO J*. **22** (12): 2913–23. [doi](/source/Doi_(identifier)):[10.1093/emboj/cdg299](https://doi.org/10.1093%2Femboj%2Fcdg299). [PMC](/source/PMC_(identifier)) [162151](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC162151). [PMID](/source/PMID_(identifier)) [12805207](https://pubmed.ncbi.nlm.nih.gov/12805207).

- Brown AM, Gordon D, Lee H, et al. (2004). "Substantial linkage disequilibrium across the dihydrolipoyl succinyltransferase gene region without Alzheimer's disease association". *Neurochem. Res*. **29** (3): 629–35. [doi](/source/Doi_(identifier)):[10.1023/B:NERE.0000014833.54481.1d](https://doi.org/10.1023%2FB%3ANERE.0000014833.54481.1d). [PMID](/source/PMID_(identifier)) [15038610](https://pubmed.ncbi.nlm.nih.gov/15038610). [S2CID](/source/S2CID_(identifier)) [35438569](https://api.semanticscholar.org/CorpusID:35438569).

- 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)"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC528928). *Genome Res*. **14** (10B): 2121–7. [doi](/source/Doi_(identifier)):[10.1101/gr.2596504](https://doi.org/10.1101%2Fgr.2596504). [PMC](/source/PMC_(identifier)) [528928](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC528928). [PMID](/source/PMID_(identifier)) [15489334](https://pubmed.ncbi.nlm.nih.gov/15489334).

- Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". *Cell*. **122** (6): 957–68. [doi](/source/Doi_(identifier)):[10.1016/j.cell.2005.08.029](https://doi.org/10.1016%2Fj.cell.2005.08.029). [hdl](/source/Hdl_(identifier)):[11858/00-001M-0000-0010-8592-0](https://hdl.handle.net/11858%2F00-001M-0000-0010-8592-0). [PMID](/source/PMID_(identifier)) [16169070](https://pubmed.ncbi.nlm.nih.gov/16169070). [S2CID](/source/S2CID_(identifier)) [8235923](https://api.semanticscholar.org/CorpusID:8235923).

- Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". *Nature*. **437** (7062): 1173–8. [Bibcode](/source/Bibcode_(identifier)):[2005Natur.437.1173R](https://ui.adsabs.harvard.edu/abs/2005Natur.437.1173R). [doi](/source/Doi_(identifier)):[10.1038/nature04209](https://doi.org/10.1038%2Fnature04209). [PMID](/source/PMID_(identifier)) [16189514](https://pubmed.ncbi.nlm.nih.gov/16189514). [S2CID](/source/S2CID_(identifier)) [4427026](https://api.semanticscholar.org/CorpusID:4427026).

v t e Enzymes: multienzyme complexes Photosynthesis Photosynthetic reaction center complex proteins Photosystem I II Dehydrogenase 2-oxoadipate dehydrogenase complex DHTKD1 DLST DLD Branched-chain alpha-keto acid dehydrogenase complex BCKDHA BCKDHB DBT DLD Pyruvate dehydrogenase complex PDH DLAT DLD PDHX Oxoglutarate dehydrogenase OGDH DLST DLD Other CAD Carbamoyl phosphate synthase II Aspartate carbamoyltransferase Dihydroorotase P450-containing systems Cytochrome b6f complex Electron transport chain Fatty acid synthetase complex Glycine decarboxylase complex Mitochondrial trifunctional protein HADHA HADHB Phosphoenolpyruvate sugar phosphotransferase system Polyketide synthase Sucrase-isomaltase complex Tryptophan synthase

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Adapted from the Wikipedia article [DLST](https://en.wikipedia.org/wiki/DLST) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/DLST?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.