The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Chemical Compound Review

succinyl-CoA     3-[2-[3-[[(2R)-4- [[[(2R,3S,4R,5R)-5-(6...

Synonyms: CHEBI:15380, AC1L3NHJ, C00091, 604-98-8, SCA, ...
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of Succinyl-coenzyme A

 

High impact information on Succinyl-coenzyme A

 

Biological context of Succinyl-coenzyme A

 

Anatomical context of Succinyl-coenzyme A

 

Associations of Succinyl-coenzyme A with other chemical compounds

 

Gene context of Succinyl-coenzyme A

  • Succinyl coenzyme A synthetase and Ndk form a complex in P. aeruginosa [16].
  • Methylmalonyl-coenzyme A mutase (MCM) is a 5'-deoxyadenosylcobalamin-linked mitochondrial enzyme that catalyzes the isomerization of L-methylmalonyl-coenzyme A to succinyl-coenzyme A [17].
  • (Ebert, P.S., Tschudy, D.P., Choudhry, J.N. and Chirigos, M.A. (1970) Biochim. Biophys. Acta 208, 236--250) can yield erroneous results with succinyl-coenzyme A as substrate, especially when incubations are carried out for less than 25 min [18].
  • The conversion of succinyl-coenzyme A (CoA) into methylmalonyl-CoA, catalyzed by adenosylcobalamin-dependent methylmalonyl-CoA mutase (MCM), represents an important source of building blocks for rifamycin SV biosynthesis [19].

References

  1. Capacity for alternating sites cooperativity in catalysis by succinyl-coenzyme A synthetase. Wolodko, W.T., O'Connor, M.D., Bridger, W.A. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  2. Characterization of the genes encoding beta-ketoadipate: succinyl-coenzyme A transferase in Pseudomonas putida. Parales, R.E., Harwood, C.S. J. Bacteriol. (1992) [Pubmed]
  3. Regulation of citrate synthase from blue-green bacteria by succinyl coenzyme A. Lucas, C., Weitzman, P.D. Arch. Microbiol. (1977) [Pubmed]
  4. The mechansim of action of coenzyme B12. The role thioester in a nonenzyme model reaction for coenzyme B12 Dependent isomerization of methylmalony coenzyme A to succinyl coenzyme A. Scott, A.I., Kang, K. J. Am. Chem. Soc. (1977) [Pubmed]
  5. Global analysis of proteins synthesized by Mycobacterium smegmatis provides direct evidence for physiological heterogeneity in stationary-phase cultures. Blokpoel, M.C., Smeulders, M.J., Hubbard, J.A., Keer, J., Williams, H.D. J. Bacteriol. (2005) [Pubmed]
  6. Succinyl coenzyme A synthetase of Pseudomonas aeruginosa with a broad specificity for nucleoside triphosphate (NTP) synthesis modulates specificity for NTP synthesis by the 12-kilodalton form of nucleoside diphosphate kinase. Kapatral, V., Bina, X., Chakrabarty, A.M. J. Bacteriol. (2000) [Pubmed]
  7. Metabolic pathways for cytotoxic end product formation from glutamate- and aspartate-containing peptides by Porphyromonas gingivalis. Takahashi, N., Sato, T., Yamada, T. J. Bacteriol. (2000) [Pubmed]
  8. Aerobic regulation of the sucABCD genes of Escherichia coli, which encode alpha-ketoglutarate dehydrogenase and succinyl coenzyme A synthetase: roles of ArcA, Fnr, and the upstream sdhCDAB promoter. Park, S.J., Chao, G., Gunsalus, R.P. J. Bacteriol. (1997) [Pubmed]
  9. Localization of the gene (OGDH) coding for the E1k component of the alpha-ketoglutarate dehydrogenase complex to chromosome 7p13-p11.2. Szabo, P., Cai, X., Ali, G., Blass, J.P. Genomics (1994) [Pubmed]
  10. Molecular characterization of the alpha-subunit of Trichomonas vaginalis hydrogenosomal succinyl CoA synthetase. Lahti, C.J., Bradley, P.J., Johnson, P.J. Mol. Biochem. Parasitol. (1994) [Pubmed]
  11. Neurologic degeneration associated with nitrous oxide anesthesia in patients with vitamin B12 deficiency. Flippo, T.S., Holder, W.D. Archives of surgery (Chicago, Ill. : 1960) (1993) [Pubmed]
  12. A novel mutation in the dihydrolipoamide dehydrogenase E3 subunit gene (DLD) resulting in an atypical form of alpha-ketoglutarate dehydrogenase deficiency. Odièvre, M.H., Chretien, D., Munnich, A., Robinson, B.H., Dumoulin, R., Masmoudi, S., Kadhom, N., Rötig, A., Rustin, P., Bonnefont, J.P. Hum. Mutat. (2005) [Pubmed]
  13. Ketone-body metabolism in hyperthyroid rats: reduced activity of D-3-hydroxybutyrate dehydrogenase in both liver and heart and of succinyl-coenzyme A: 3-oxoacid coenzyme A-transferase in heart. Lippolis, R., Altamura, N., Landriscina, C. Arch. Biochem. Biophys. (1988) [Pubmed]
  14. Congenital methylmalonic acidemia: a variant of the B12 'non-responsive' form with evidence for reduced affinity of methylmalonyl-CoA mutase for its B12-coenzyme. Baumgartner, E.R., Bachmann, C., Wick, H. Enzyme (1976) [Pubmed]
  15. Modulation of B12 dosage and response in fetal treatment of methylmalonic aciduria (MMA): titration of treatment dose to serum and urine MMA. Evans, M.I., Duquette, D.A., Rinaldo, P., Bawle, E., Rosenblatt, D.S., Whitty, J., Quintero, R.A., Johnson, M.P. Fetal. Diagn. Ther. (1997) [Pubmed]
  16. Regulation of nucleoside diphosphate kinase and secretable virulence factors in Pseudomonas aeruginosa: roles of algR2 and algH. Schlictman, D., Kubo, M., Shankar, S., Chakrabarty, A.M. J. Bacteriol. (1995) [Pubmed]
  17. Comparison of two methods for the measurement of rat liver methylmalonyl-coenzyme A mutase activity: HPLC and radioisotopic assays. Gaire, D., Sponne, I., Droesch, S., Charlier, A., Nicolas, J.P., Lambert, D. J. Nutr. Biochem. (1999) [Pubmed]
  18. Enzymatic degradation of succinyl-coenzyme A by rat liver homogenates. Minaga, T., Sharma, M.L., Kun, E., Piper, W.N. Biochim. Biophys. Acta (1978) [Pubmed]
  19. Molecular analysis and heterologous expression of the gene encoding methylmalonyl-coenzyme A mutase from rifamycin SV-producing strain Amycolatopsis mediterranei U32. Zhang, W., Yang, L., Jiang, W., Zhao, G., Yang, Y., Chiao, J. Appl. Biochem. Biotechnol. (1999) [Pubmed]
 
WikiGenes - Universities