The two pathways for effective orthogonal protection of L-ornithine, for amino acylation of 5'-O-pivaloyl nucleosides, describe the general and important role for the successful imitation, during the model substrates for the ribosomal mimic reaction.

Bz(NO(2))-Orn(Boc)-OCH(2)CN was synthesized as an amino acid component with effective and successful orthogonal protection for amino acylation of 5'-O-Pivaloyl nucleosides and preparation of substrates for model ribosome reactions. The synthesis was carried out using suitable combinations of the methods of peptide synthesis and modification of amino acids.

Design and synthesis of substrates for model ribosomal reactions.

2'/3'-O-[Bz(NO(2))-Orn(Boc)]-5'-O-Piv-Ado (1) and its deoxy analog: 3'-O-[Bz(NO(2))-Orn(Boc)]-5'-O-Piv-2'-dAdo (2) were designed and synthesized as substrates for the model ribosome reaction we used to demonstrate the crucial role of A76 2'-OH of peptidyl-tRNA in the rate acceleration of peptide bond formation during protein biosynthesis.

The syn-oriented 2-OH provides a favorable proton transfer geometry in 1,2-diol monoester aminolysis: implications for the ribosome mechanism.

A computational study of 1-formyl 1,2-ethanediol aminolysis predicts a stepwise mechanism involving syn-2-OH-assisted proton transfer. The syn-oriented 2-OH takes over the catalytic role of the external water or amine molecule previously observed in 2-deoxy ester aminolysis. It provides more favorable, that is, more linear, proton transfer geometry for the rate-limiting transition state resulting in an almost billion-fold rate acceleration of the overall reaction.

Theoretical study of the o-OH participation in catechol ester ammonolysis.

The possible catalytic effect of the vicinal hydroxyl group during the ammonolysis of acetylcatechol has been studied by first principle calculations. A very efficient intramolecular catalysis was found to occur when the catechol ester o-OH group is deprotonated: the activation energy of the ammonolysis decreases by 24 kcal mol(-1) as compared to that of acetylphenol ammonolysis. Using this value, the o-oxyanion-catalysed intramolecular ammonolysis was estimated to be orders of magnitude faster than the ammonolysis of acetylphenol or nonionised acetylcatechol.

Beta-aspartylpeptides as substrates of L-asparaginases from Escherichia coli and Erwinia chrysanthemi.

L-Asparaginase is known to catalyze the hydrolysis of L-asparagine to L-aspartic and ammonia, but little is known about its action on peptides. When we incubated L-asparaginases purified either from Escherichia coli or Erwinia chrysanthemi - commonly used as chemotherapeutic agents because of their antitumour activity - with eight small beta-aspartylpeptides such as beta-aspartylserineamide, beta-aspartylalanineamide, beta-aspartylglycineamide and beta-aspartylglycine, we found that both L-asparaginases could catalyze the hydrolysis of five of them yielding L-aspartic acid and amino acids or peptides. Our data show that L-asparaginases can hydrolyze beta-aspartylpeptides and suggest that L-asparaginase therapy may affect the metabolism of beta-aspartylpeptides present in human body.