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D-Alanine Metabolism in S. pomeroyi

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The Alpha-Proteobacteria is predominantly responsible for the degradation of organosulfur compounds, including the algal osmolyte dimethylsulfoniopropionate. Silicobacter pomeroyi carries out many organic sulfur transformations that occur in natural bacterial communities in the surface ocean. The bacterium converts dimethylsulfoniopropionate to both dimethylsulfide and methanethiol. Through these pathways, the sulfur in dimethylsulfoniopropionate is either released as volatile sulfur to the atmosphere, or retained in the marine food web in the form of S-containing amino acids (Ref.1 & 2). The cell wall of these bacteria is a unique biopolymer, containing both D- and L-Amino acids. The terminal peptide is D-Alanine although other amino acids are present as D-isomers and this is the only known biological molecule that contains D-Amino acids, which are responsible [...]


1.Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine environment.
Moran MA, Buchan A, Gonzalez JM, Heidelberg JF, Whitman WB, Kiene RP, Henriksen JR, King GM, Belas R, Fuqua C, Brinkac L, Lewis M, Johri S, Weaver B, Pai G, Eisen JA, Rahe E, Sheldon WM, Ye W, Miller TR, Carlton J, Rasko DA, Paulsen IT, Ren Q, Daugherty SC, Deboy RT, Dodson RJ, Durkin AS, Madupu R, Nelson WC, Sullivan SA, Rosovitz MJ, Haft DH, Selengut J, Ward N.
Nature. 2004 Dec 16;432(7019):910-3.
2.Silicibacter pomeroyi sp. nov. and Roseovarius nubinhibens sp. nov.,dimethylsulfoniopropionate-demethylating bacteria from marine environments.
Gonzalez JM, Covert JS, Whitman WB, Henriksen JR, Mayer F, Scharf B, Schmitt R, Buchan A, Fuhrman JA, Kiene RP, Moran MA.
Int J Syst Evol Microbiol. 2003 Sep;53(Pt 5):1261-9.
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