SUCLA2

From Wikipedia, the free encyclopedia

Succinate-CoA ligase, ADP-forming, beta subunit

Identifiers

External IDs

OMIM: 603921 MGI: 1306775 HomoloGene: 2856

Gene ontology
Molecular Function:	• catalytic activity • succinate-CoA ligase (ADP-forming) activity • protein binding • ATP binding • ligase activity
Cellular Component:	• mitochondrion
Biological Process:	• tricarboxylic acid cycle • succinyl-CoA pathway • metabolic process

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_003850 (mRNA)
NP_003841 (protein)

NM_011506 (mRNA)
NP_035636 (protein)

Location

n/a

Chr 14: 72.29 - 72.33 Mb

Pubmed search

[1]

[2]

Succinate-CoA ligase, ADP-forming, beta subunit, also known as SUCLA2, is a human gene.^[1]

The SUCLA2 gene encodes the beta-subunit of the ADP-forming succinyl-CoA synthetase (SCS-A; EC 6.2.1.5). SCS is a mitochondrial matrix enzyme that catalyzes the reversible synthesis of succinyl-CoA from succinate and CoA. The reverse reaction occurs in the Krebs cycle, while the forward reaction may produce succinyl-CoA for activation of ketone bodies and heme synthesis. GTP-specific (SCS-G; EC 6.2.1.4) and ATP-specific (SCS-A) isoforms of SCS catalyze GTP-dependent and ATP-dependent reactions, respectively. SCS is composed of an invariant alpha subunit and a beta subunit that determines the enzyme's nucleotide specificity.[supplied by OMIM]^[1]

[edit] References

^ ^a ^b Entrez Gene: SUCLA2 succinate-CoA ligase, ADP-forming, beta subunit.

[edit] Further reading

Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
Johnson JD, Mehus JG, Tews K, et al. (1998). "Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA synthetases in multicellular eucaryotes.". J. Biol. Chem. 273 (42): 27580–6. PMID 9765291.
Scanlan MJ, Gordan JD, Williamson B, et al. (1999). "Antigens recognized by autologous antibody in patients with renal-cell carcinoma.". Int. J. Cancer 83 (4): 456–64. PMID 10508479.
Furuyama K, Sassa S (2000). "Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is disrupted in sideroblastic anemia.". J. Clin. Invest. 105 (6): 757–64. PMID 10727444.
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. PMID 12477932.
Cox TC, Sadlon TJ, Schwarz QP, et al. (2004). "The major splice variant of human 5-aminolevulinate synthase-2 contributes significantly to erythroid heme biosynthesis.". Int. J. Biochem. Cell Biol. 36 (2): 281–95. PMID 14643893.
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.
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. PMID 15489334.
Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455.
Elpeleg O, Miller C, Hershkovitz E, et al. (2005). "Deficiency of the ADP-forming succinyl-CoA synthase activity is associated with encephalomyopathy and mitochondrial DNA depletion.". Am. J. Hum. Genet. 76 (6): 1081–6. doi:10.1086/430843. PMID 15877282.
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. doi:10.1038/nature04209. PMID 16189514.