Amino acid synthesis enzyme multiplicity

Now we will return briefly to Sections 3.8-3.11 and 4.6-4.8 where we considered the general problem of multiple flows, here of H, C, N, O, S and P. We observe immediately that all the products are from the same small molecule environmental sources and are required to be formed in relatively fixed amounts using the same source of energy and a series of intermediates. Controlling all the processes to bring about optimum cellular production are feedbacks between them and linked with the code which generates proteins, and here we note particularly enzymes, i.e. catalysts. The catalysts are made from the amino acids, the synthesis of which they themselves manage, while the amino acids control the catalysts so as to maintain a restricted balanced set of reaction pathways in an autocatalytic assembly. It is also the feedback controls on both the DNA (RNA) from the same units used in the... 

In Section 5.03.6.2, a stereoselective synthesis of L-homophenylalanine from the racemic AAacetylated amino acid is described. The authors, however, found that substrate solubility limited the utility of this procedure. Having found an L-N-carbamoylase in Bacillus kaustophilus, they introduced the gene for this enzyme together with that for the N-acyl amino acid racemase from D. radiodurans into E. coli for coexpression. These cells, permeabilized with 0.5% toluene, were able to deliver L-homophenylalanine in 99% yield and were able to be used for multiple reaction cycles. 

The synthesis of microginin, an angiotension converting enzyme inhibitory pentapeptide, involves the multiple steps wherein DEPC is used as coupling agent.73 A key component 193 required for the synthesis of microginin is obtained from N-protected amino acid (191) and amine 192. 

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