DLST

Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial is an enzyme that in humans is encoded by the DLST gene.^[5][6]

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 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

Interactive pathway map

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

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|alt=TCACycle_WP78 edit]]

TCACycle_WP78 edit

1. The interactive pathway map can be edited at WikiPathways: "TCACycle_WP78".

References

1. GRCh38: Ensembl release 89: ENSG00000119689 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000004789 – 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. 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:10.1007/BF02290679. PMID 8009371. S2CID 43092605.
6. "Entrez Gene: DLST dihydrolipoamide S-succinyltransferase (E2 component of 2-oxo-glutarate complex)".

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 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". Hepatology. 11 (6): 975–81. doi:10.1002/hep.1840110611. PMID 2365294. S2CID 83760368.
• Ono K, Hakozaki M, Kimura A, Kochi H (1987). "Purification, resolution, and reconstitution of rat liver branched-chain alpha-keto acid dehydrogenase complex". J. Biochem. 101 (1): 19–27. doi:10.1093/oxfordjournals.jbchem.a121891. PMID 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:10.1016/0003-9861(86)90002-0. PMID 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". Eur. J. Biochem. 224 (1): 179–89. doi:10.1111/j.1432-1033.1994.tb20010.x. PMID 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:10.1006/bbrc.1993.2282. PMID 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:10.1016/0167-4781(93)90002-u. PMID 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". Neurosci. Lett. 199 (1): 73–7. doi:10.1016/0304-3940(95)11982-3. hdl:1765/72164. PMID 8584231. S2CID 7439684.
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 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:10.1006/bbrc.1997.7784. PMID 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". J. Biol. Chem. 273 (37): 24158–64. doi:10.1074/jbc.273.37.24158. PMID 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:10.1002/1531-8249(199901)45:1<48::AID-ART9>3.0.CO;2-V. PMID 9894876. S2CID 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 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". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Kanamori T, Nishimaki K, Asoh S, et al. (2003). "Truncated product of the bifunctional DLST gene involved in biogenesis of the respiratory chain". EMBO J. 22 (12): 2913–23. doi:10.1093/emboj/cdg299. PMC 162151. PMID 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:10.1023/B:NERE.0000014833.54481.1d. PMID 15038610. S2CID 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)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 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:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 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:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.