Amino acids, syntheses properties

Yang J, Alemany LB, Driver J, Hartgerink JD, Barron AR (2007a) Fullerene-derivatized amino acids Synthesis, characterization, antioxidant properties, and solid-phase peptide synthesis. Chem. Eur. J. 13 2530-2545. 

Kuhkar, V. P Soloshonok, V. A. Fluorine-Containing Amino Acids Synthesis and Properties Wiley Chichester, U.K., 1995. 

Amino Acids, Chemical Properties of Click Peptides, Design and Application of Peptide Combinatorial Libraries Solid-Phase Synthesis of Biomolecules... 

Greenstein, J. P. and Winitz, M. (1961) Chemistry of the Amino Acids, Wiley, New York. Kukhar, V. P. and Soloshonok, V. A. (Ed.) (1995) Fluorine-Containing Amino Acids Synthesis and Properties, Wiley, Chichester. 

In Klebsiella terrigena and Bacillus subtilis, this enzyme is found within the acetoin cluster of genes. Interestingly, in Lactobacillus lactis, this gene is found within the gene cluster that encodes the enzymes of branched chain amino acid synthesis. This enzyme has different kinetic properties than the enzymes of K. terrigena and B. subtilis and may play a key role in acetolactate flux in L. lacHs (Goupil-Feuillerat et al. 1997). 

Fluorine-containing Amino Acids. Synthesis and Properties Kukhar, V. P. Soloshonok, V. A., Eds. John Wiley Sons Chichester, 1994. 

Frontiers of Fluorine Chemistry ACS Books, ACS Washington, D. C., 1996. (b) Resnati, G. Soloshonok, V. A. Eds. Tetrahedron Symposia-in-Print 1996, 52, No. 1. (c) Kukhar, V. P. Soloshonok, V. A. Eds. Fluorine-containing Amino Acids Synthesis and Properties John Wiley Sons Chichester, 1995. (d) Hudlicky, M. Pavlath, A. E. 

Of the enzymes associated with aromatic amino acid biosynthesis, there is good evidence that unique isozymes of DAHP (Rubin and Jensen, 1985), chorismate synthetase (d Amato et al 1984), and anthranilate synthase (Brotherton et ai, 1986) are differentially localized within chloroplasts and in the cytoplasm. The regulatory properties of the plastid isozymes are consistent with their involvement in amino acid synthesis. Many of the remaining pathway enzymes have also been detected in plastids, including all those required for the synthesis of EPSP [(1) to (6)] (Mousdale and Coggins, 1985). These results, combined with those obtained during measurements of the biosynthetic capabilities of isolated chloroplasts (Bickel and Schultz, 1979 Buchholz and Schultz, 1980 Schulze-Siebert et ai, 1984), leave little doubt that these organelles are a primary site of aromatic amino acid biosynthesis. 

In many cases only the racemic mixtures of a-amino acids can be obtained through chemical synthesis. Therefore, optical resolution (42) is indispensable to get the optically active L- or D-forms in the production of expensive or uncommon amino acids. The optical resolution of amino acids can be done in two general ways physical or chemical methods which apply the stereospecific properties of amino acids, and biological or enzymatic methods which are based on the characteristic behavior of amino acids in living cells in the presence of enzymes. 

---