It has been hypothesized that cysteamine, which is a chemical pre

It has been hypothesized that cysteamine, which is a chemical precursor of the pantetheine moiety of coenzyme A, was formed in the primitive oceans from ethylene sulfide and ammonia or from ethylene imine and hydrogen sulfide (Keefe et al. 1995). However, our results suggest that cysteamine could have also formed readily from electric discharges. The recently discovered enzymatic conversion of cysteate into sulfopyruvate in the biosynthesis of coenzyme M (2-mercaptoethanesulfonic acid, HSCH2CH2SO3H) in Methanosarcina acetivorans (Graham et al. 2009) supports the idea that products of cysteine degradation and

other sulfur-bearing organic compounds SB-715992 concentration of prebiotic origin may have been involved in early selleck chemicals biological processes. The selection of the two thio-amino acids present in proteins is likely the outcome of a combination of their availability coupled with their functional utility (Cleaves 2010; Weber and Miller 1981). It has been suggested that cysteine could be an evolutionary replacement of an ancestral sulfhydryl-containing coenzyme (White 1982). However, it is possible that cysteine was first incorporated into proteins because of its ability to form RNA-recognizing zinc-fingers, to bind to Fe/S clusters and to dimerize and covalently link to form disulfide bonds that play a key role in maintaining functional three-dimensionally folded

protein structures. In addition to its role as a building block in proteins, methionine is the immediate SN-38 precursor

of S-adenosylmethionine (SAM), the major methyl-group donor in transmethylation reactions in contemporary biochemistry. It has been proposed that methyl group transfer from SAM to amines may be vestigial of prebiotic Avelestat (AZD9668) methylation reactions involving formaldehyde (Waddell et al. 2000). However, the possibility that ribonucleotide-like coenzymes are remnants of an ancestral stage in which ribozymes played a more conspicuous role in metabolism (Orgel and Sulston 1971; White 1976) suggests that methionine may have been first incorporated into biological systems because of its involvement in methyltransferase activities that evolved in a primordial RNA-dependent world. In other words, it is possible that methionine was initially incorporated into the RNA world as a cofactor. Acknowledgements We are grateful to the librarians of the Mandeville Special Collections in the Geisel Library at the University of California, San Diego campus. Support from a UC Mexus-CONACYT Fellowship to A.L. and the NASA Astrobiology Institute and Goddard Center for Astrobiology for J.P.D. and D.P.G. are gratefully acknowledged. H.J.C. and M.P.C. were supported by the NASA Post-Doctoral Program (NPP). We also thank Dr. Jamie Elsila for GC-MS analyses of these extracts and Professor Facundo Fernandez for DART-ToF analyses.

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