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Is there strong or weak correlation between conservation of sequence and structure, the mode of SAM binding, and the chemical reaction facilitated by the enzyme?Finally, what may have been the repertoire of SAM-binding proteins in the ancestral organisms – in particular, in LUCA, the Last Universal Common Ancestor of the three present-day domains of Life – Bacteria, Archaea, and Eukarya?
Methyl transfer is but one of many biochemical processes requiring SAM.
Enzymatic reactions that involve interaction of proteins with SAM or its structurally similar derivatives include transfer or methylene, aminoalkyl, ribosyl, and 5'deoxyadenosyl groups; formation of 5'deoxyadenosyl radical, which can be used as a redox intermediate in many reactions; SAM decarboxylation; and synthesis of SAM from adenosine and methionine.
Several classes of proteins have unique unrelated folds, specialized for just one type of chemistry and unified by the theme of internal domain duplications.
In several cases, functional divergence is evident, when evolutionarily related enzymes have changed the mode of binding and the type of chemical transformation of -adenosylmethionine-binding proteins.
Comparison of remote sequence similarities and analysis of phyletic patterns suggests that the last universal common ancestor of cellular life had between 10 and 20 We have observed several novel relationships between families that were not known to be related before, and defined 15 large superfamilies of SAM-binding proteins, at least 5 of which may have been represented in the last common ancestor.