Light chains biosynthesis

Williamson, A. R., and B. A. Askonas. 1967. Biosynthesis of immunoglobulins the separate classes of polyribosomes synthesizing heavy and light chains. J. Molec. Biol., 23 201-215. 

Figure 4.7 Two of the enzymatic activities involved in the biosynthesis of tryptophan in E. coli, phosphoribosyl anthranilate (PRA) isomerase and indoleglycerol phosphate (IGP) synthase, are performed by two separate domains in the polypeptide chain of a bifunctional enzyme. Both these domains are a/p-barrel structures, oriented such that their active sites are on opposite sides of the molecule. The two catalytic reactions are therefore independent of each other. The diagram shows the IGP-synthase domain (residues 48-254) with dark colors and the PRA-isomerase domain with light colors. The a helices are sequentially labeled a-h in both barrel domains. Residue 255 (arrow) is the first residue of the second domain. (Adapted from J.P. Priestle et al., Proc.

Altohyrtin C, which involved the synthesis of ylide (90) that contains the said side chain,and Xerulin, which inhibits the biosynthesis of cholesterol, which required the use of ylide (91). Wittig reactions are also useful reagents for the synthesis of polymeric materials, for example fluorene ylide (92) has been used to generate light emitting polymers. ... 

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