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Escherichia coli cloning system

Recently, a potential cytosolic component of the MEP precursor pathway, xylulose kinase, has been cloned and tested for function in an Escherichia coli complementation system. " The kinase activates exogenous xylulose in the cytoplasm. DXP is the precursor for DXS, which resides in the plastid, suggesting the activated substrate must be transported into the plastid. Another xylulose kinase homologue in Arabidopsis that contains a plastid targeting sequence was not active in the E. coli system, suggesting that it may have some other function in the plastid. Perhaps plant and bacterial tissue cultures may be fed xylulose to condition accumulation of isoprenoid metabolites. [Pg.360]

Ashiuchi M, Soda K, Misono H. (1999). A poly-y-glutamate synthetic system of Bacillus subtilis IFO 3336 gene cloning and biochemical analysis of poly-y-glutamate produced by Escherichia coli clone cells. Biochem Biophys Res Commun, 263, 6-12. [Pg.489]

A recombinant Escherichia coli strain containing the cloned limonene hydratase gene was able to grow in a water-limonene two-phase system and converted limonene to a-terpineol [36], Limonene, a cost-effective and readily available monoterpene, served both as the substrate and the neat solvent for the production of a-terpineol. [Pg.237]

The biocatalytic reduction of carboxylic acids to their respective aldehydes or alcohols is a relatively new biocatalytic process with the potential to replace conventional chemical processes that use toxic metal catalysts and noxious reagents. An enzyme known as carboxylic acid reductase (Car) from Nocardia sp. NRRL 5646 was cloned into Escherichia coli BL21(DE3). This E. coli based biocatalyst grows faster, expresses Car, and produces fewer side products than Nocardia. Although the enzyme itself can be used in small-scale reactions, whole E. coli cells containing Car and the natural cofactors ATP and NADPH, are easily used to reduce a wide range of carboxylic acids, conceivably at any scale. The biocatalytic reduction of vanillic acid to the commercially valuable product vanillin is used to illustrate the ease and efficiency of the recombinant Car E. coli reduction system." A comprehensive overview is given in Reference 6, and experimental details below are taken primarily from Reference 7. [Pg.295]

Saffen, D.W. Presper, K.A. Doering, T.L. Roseman, S. Sugar transport by the bacterial phosphotransferase system. Molecular cloning and structural analysis of the Escherichia coli ptsH, ptsi, and err genes. J. Biol. Chem., 262, 16241-16253 (1987)... [Pg.421]

Chauvin, F. Fomenkov, A. Johnson, C.R. Roseman, S. The N-terminal domain of Escherichia coli enzyme I of the phosphoenolpyruvate/glycose phosphotransferase system molecular cloning and characterization. Proc. Natl. Acad. Sci.USA, 93, 7028-7031 (1996)... [Pg.421]

Cloning in Systems Other than Escherichia coli Site-Directed Mutagenesis Permits the Restructuring of Existing Genes... [Pg.678]

Cloning in Systems Other than Escherichia coli... [Pg.688]

Abstract The multi-step enzyme catalysed biosyntheses of monoterpenoid indole and isoquinoline alkaloids are described. Special emphasis is placed on those pathways leading to alkaloids of pharmacological and medicinal significance which have been fully elucidated at the enzyme level. The successful identification and cloning of cDNAs of single enzymes and their application provides great opportunities to develop novel strategies for both in vitro and in vivo alkaloid production in whole plants or tissue cultures, as well as in microbial systems such as Escherichia coli and yeast. [Pg.67]

Takahashi et al.61s further identified the primary structure by preparing a cDNA library from A. fumigatus induced with fructosylpropylamine and isolated a clone using a polyclonal Amadoriase II antibody. The structure comprised 438 amino acid residues, corresponding to 48.798 kDa. The identity of the Amadoriase n cDNA was further confirmed by expression in Escherichia coli cells with an inducible expression system. Northern-blotting analysis showed that Amadoriase II was induced by fructosylpropylamine in a dose-dependent manner. The sequence determined showed the enzyme to represent a new family of mammalian enzymes. The sequence exhibited 82 and 36% identity and 92 and 65% similarity, respectively, with the two sequences determined by Yoshida et al.616 Amadori products have been implicated in the formation of H202, but the in vivo mechanism needs to be elucidated further. [Pg.169]


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See also in sourсe #XX -- [ Pg.22 ]




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Escherichia coli cloning

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