doi: 10.1007/BF00450664.
Evolutionary constraints in the mechanism of flavin catalysis
- PMID: 7442813
- DOI: 10.1007/BF00450664
Item in Clipboard
Evolutionary constraints in the mechanism of flavin catalysis
Naturwissenschaften.
1980 Nov.
Abstract
Analysis of the possible evolution of flavin catalysis in succinate dehydrogenase suggests as the ultimate state an active site that bears one or more acid functions and uses the enediol form of the substrate rather than the carbanion as a nucleophile. In the case of flavoenzyme catalyzed oxidation of fatty acylCoA, alpha-amino acids and alpha-hydroxy acids evolution to a similar mechanism seems to be blocked.
Similar articles
-
Evolutionary roots of catalysis by nicotinamide and flavins in C-H oxidoreductases and in photosynthesis.Orig Life. 1982 Jun;12(2):165-79. doi: 10.1007/BF00927143. Orig Life. 1982. PMID: 6216447
-
Modification of the thermodynamic properties of the electron-transferring groups in mitochondrial succinate dehydrogenase upon binding of succinate.Eur J Biochem. 1983 Aug 15;134(3):439-45. doi: 10.1111/j.1432-1033.1983.tb07586.x. Eur J Biochem. 1983. PMID: 6884342
-
Modulation of the flavin redox potential as mode of regulation of succinate dehydrogenase activity.Biochim Biophys Acta. 1980 Jul 8;591(2):400-8. doi: 10.1016/0005-2728(80)90171-1. Biochim Biophys Acta. 1980. PMID: 7397131
-
Succinate dehydrogenase.Adv Enzymol Relat Areas Mol Biol. 1973;37:189-272. doi: 10.1002/9780470122822.ch4. Adv Enzymol Relat Areas Mol Biol. 1973. PMID: 4570066 Review. No abstract available.
-
The reductive half reaction in the acyl-CoA dehydrogenases.Prog Clin Biol Res. 1990;321:91-105. Prog Clin Biol Res. 1990. PMID: 2183245 Review. No abstract available.
Cited by
-
Evolutionary roots of catalysis by nicotinamide and flavins in C-H oxidoreductases and in photosynthesis.Orig Life. 1982 Jun;12(2):165-79. doi: 10.1007/BF00927143. Orig Life. 1982. PMID: 6216447