Abstract
Biosynthesis of peptides requires (1) carboxyl group activation, and (2) specific addition of acceptor amino (imino) group. Activation reactions include formation of phosphates (peptidoglycan, glutathione) or of adenylates (aminoacyl-tRNA-ligases, gramicidin S-synthetase). Ami-noacyl compounds may be stabilized as tRNA-esters or enzyme thioesters (pantetheine-mediated peptide synthesis), while CoA-derivatives of amino acids have not been observed. Addition reactions generally involve recognition of two substrates (containing donor and acceptor group) by protein structures. Evidence for a linear template regulating the sequence of events has so far only been found in mRNA in the ribosomal system. A scheme for discussion of these reactions is given in Fig. 1.
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