Escherichia coli protein biosynthesis

Armstrong SK, Pettis CS, Forrester LJ, McIntosh MA. The Escherichia coli enterobactin biosynthesis gene, entD Nucleotide sequence and membrane localization of its protein prod-uct. Mol Microbiol 1989 3 757-766. 

Rohdich, F., Wungsintaweekul, J., Fellermeier, M. et al. (1999) Cytidine 5 -triphosphate-dependent biosynthesis of isoprenoids YgbP protein of Escherichia coli catalyzes the formation of 4-diphosphocy-tidyl-2-C-methylerythritol. Proceedings of the National Academy of Sciences of the United States of America, 96, 11758-11763. 

LUTTGEN, H ROHDICH, F., HERZ, S., WUNGSINTAWEEKUL, J., HECHT, S., SCHUHR, C.A., FELLERMEIER, M., SAGNER, S., ZENK, M.H., BACHER, A., EISENREICH, W., Biosynthesis of terpenoids ychB protein of Escherichia coli phosphorylates the 2-hydroxy group of 4-diphosphocytidyl-2-C-methyl-D-erythritol, Proc. Natl. Acad. Sci. USA, 2000,97,1062-1067. 

Xi, J., Ge, Y., Kinsland, C., McLaeeerty, F. W., and Begley, T. P. Biosynthesis of the thiazole moiety of thiamin in Escherichia coli identification of an acyldisulfide-linked protein-protein conjugate that is fimctionally analogous to the ubiquitin/El complex, Proc Natl Acad Sci USA 2001, 98, 8513-8518. 

ImHNL is a nonglycosylated homodimer (84 kDa) which catalyzes the reversible cleavage of aliphatic (R)-cyanohydrins [34]. This HNL does not require complex protein modification after protein biosynthesis. Thus, expression in prokaryotic Escherichia coli) and eukaryotic hosts Pichia pastoris) is possible [35-37]. However, initial trials to express IwHNL in E. coli were hampered by formation of inclusion bodies [36]. 

Escherichia coli has served as the organism of choice for examining the pathways for amino acid biosynthesis for two reasons (1) E. coli synthesizes all 20 amino acids commonly found in proteins, and (2) E. coli is an organism ideally suited for genetic and biochemical studies. 

Relatively recently Fe/S proteins have been found to function in the regulation of biosynthesis. This can be by promoting deoxyribonucleic acid (DNA) transcription, e.g. the [2Fe-2S] containing Escherichia coli superoxide-activated (SoxR) transcription activator [10-12], or the presumably [4Fe-4S]-containing E. coli transcription factor fumarate nitrate reduction (FNR) [13,14], Alternatively, the Fe/S protein can act by interference with messenger ribonucleic acid (mRNA) translation, i.e., the iron regulatory proteins (IRPs) [15,16], These interactions are stoichiometric, therefore not catalytic. Presumably, they are also a form of sensoring, namely, of oxidants and/or iron [17],... 

Schachtschabel, D. and Zillig, W. (1959) Investigations on the biosynthesis of proteins. I. Synthesis of radiocarbon labeled amino acids in proteins of cell-free nucleoprotein-enzyme-system of Escherichia coli. Hoppe-Seyler s Z. Physiol. Chem. 314, 262-275. 

S Mohan, TM Kelly, SS Eveland, CR Raetz, MS Anderson. An Escherichia coli gene (FabZ) encoding (3R)-hydroxymyristoyl acyl carrier protein dehydrase. Relation to fabA and suppression of mutations in lipid A biosynthesis. J Biol Chem 269 32896-32903, 1994. 

Brozek, K.A., Raetz, C.R.H. Biosynthesis of lipid A in Escherichia coli acyl carrier protein-dependent incorporation of laurate and myristate. J Biol Chem 265 (1990) 15410-15417. 

Heath, R.J., Rock, C.O. Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis. J Biol Chem 271 (1996) 27795-27801. 

One example of an enzyme-catalyzed reaction involving a radical intermediate is the enzyme ribonucleotide reductase, which catalyzes the conversion of ribonucleotides (used for RNA biosynthesis) to 2 -deoxyribonucleotides (used for DNA biosynthesis), as illustrated in Fig. 16. Spectroscopic studies of the R2 subunit of Escherichia coli ribonucleotide reductase have shown that it can form a stable, long-lived, tyrosyl radical species—the first protein radical to be discovered (13). 

Furanocoumarins are extremely toxic. They are known to cause photo-toxicity if not used under medical supervision. Furanocoumarins bind to DNA of the cell and interacts with fats and proteins. Phenylalanine, Umbelliferon, a hydroxycoumarin and isoprene, are precursor compounds for furanocoumarin biosynthesis. The furanocoumarins have shown antibacterial activity against Escherichia coli and Micrococcus luteus. They are hepatotoxic also. 

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