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Escherichia coli function

Ran J, A Stolz (2003) Oxygen-insensitive nitroreductases NfsA and NfsB of Escherichia coli function under anaerobic conditions as lawsone-dependent azo reductases. Appl Environ Microbiol 69 3448-3455. [Pg.161]

Tokishita, S. Kojima, A. Mizuno, T. Transmembrane signal transduction and osmoregulation in Escherichia coli functional importance of the transmembrane regions of membrane-located protein kinase, EnvZ. J. Biochem., Ill, 707-713 (1992)... [Pg.458]

Souiri M, Gammoudi I, Ouada HB, Mora L, Jouenne T, Jaffrezic-Renault N, Dejous C, Othmane A, Duncan AC (2009) Escherichia coli-functionalized magnetic nanobeads as an ultrasensitive biosensor for heavy metals. Procedia Chem 1(1) 1027-1030. doi 10.1016/j. proche.2009.07.256... [Pg.312]

The lactose carrier of Escherichia coli functionally incorporated in Rhodopseudomonas sphaeroides obeys the regulatory conditions of the phototrophic bacterium, submitted. [Pg.353]

THE LACTOSE CARRIER OF ESCHERICHIA COLI FUNCTIONALLY INCORPORATED IN RHODOPSEUDOMONAS SPHAEROIDES OBEYS THE REGULATORY CONDITIONS OF THE PHOTOTROPHIC BACTERIUM... [Pg.469]

More than 30 years ago Jacob and Monod introduced the Escherichia coli lac operon as a model for gene regulation. The lac repressor molecule functions as a switch, regulated by inducer molecules, which controls the synthesis of enzymes necessary for E. coli to use lactose as an energy source. In the absence of lactose the repressor binds tightly to the operator DNA preventing the synthesis of these enzymes. Conversely when lactose is present, the repressor dissociates from the operator, allowing transcription of the operon. [Pg.143]

Functional proteins are also involved in high-affinity Ni transport for hydrogenase synthesis. One example is the nikABCDE gene cluster of Escherichia coli 20). NikA is a periplasmic Ni-binding protein. [Pg.286]

Even entrapment of entire cells within reversed micelles without loss of their functionality has been achieved. For example, mitochondria and bacteria (Actinobacter cal-coaceticus, Escherichia coli, Corynebacterium equi) have been successfully solubilized in a microemulsion consisting of isopropyl pahnitate, polyoxyethylene sorbitan trioleate [162], Enhanced hydrogen photoproduction by the bacterium Rhodopseudomonas sphaeroides or by the coupled system Halobacterium halobium and chloroplasts organelles entrapped inside the aqueous core of reversed micelles with respect to the same cells suspended in normal aqueous medium has been reported [183,184],... [Pg.489]

A great deal of our current understanding of the structure and function of the outer membrane of Gram-negative bacteria has come from studies with Escherichia coli and Salmonella typhimurium. The permeability barrier function of the outer membrane can... [Pg.266]

KAJIWARA S, KAKIZONO T, SAITO T, KONDO K, OHTANI T, NISHIO N, NAGAI S and MISAWA N (1995) Isolation and functional identification of a novel cDNA for astaxanthin biosynthesis from Haematococcus pluvialis, and astaxanthin synthesis in Escherichia coli . Plant Mol Biol, 29, 343-52. [Pg.276]

Expression of a tomato cDNA coding for phytoene synthase in Escherichia coli, ph)doene formation in vivo and in vitro, and functional analysis of the varions trimcated gene prodncts , J Biochem (Tokyo), 116, 980-85. [Pg.277]

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]

Linden, H. et al.. Functional complementation in Escherichia coli of different phytoene desaturase genes and analysis of accumulated carotenoids, Z. Naturforsch. 46c, 1045, 1991. [Pg.392]

Misawa, N. et al.. Elucidation of the Erwinia uredovora carotenoid biosynthetic pathway by functional analysis of gene products expressed in Escherichia coli, J. Bacteriol. 172, 6704, 1990. [Pg.392]

Cunningham, F.X. Jr. et ah. Cloning and functional expression in Escherichia coli of a cyanobacterial gene for lycopene cyclase, the enzyme that catalyzes the biosynthesis of beta-carotene, FEBS Lett. 328, 130, 1993. [Pg.393]

Quinlan, R., Jaradat, T.T., and Wurtzel, E.T., Escherichia coli as a platform for functional expression of plant P450 carotene hydroxylases. Arch. Biochem. Biophys. In press, 2006. [Pg.393]

Suits MDL, GP Pal, K Nakatsu, A Matte, M Cygler, Z Jia (2005) Identification of an Escherichia coli 0157 H7 heme oxygenase with tandem functional repeats. Proc Natl Acad USA 102 16955-16960. [Pg.145]

The conditions under which these function and their regulation depend on the organism. For example, in Escherichia coli, oxygen represses the synthesis of the other reductases, and under anaerobic conditions the reductases for fumarate, DMSO, and TMAO are repressed by nitrate. This does not apply to Wolinella succinogenes in which sulfur represses the synthesis of the more positive electron acceptors nitrate and fumarate (Lorenzen et al. 1993). The DMSO reductase from Escherichia coli (Weiner et al. 1988) has a broad substrate versatility, and is able to reduce a range of sulfoxides and A-oxides. Anaerobic sulfate reduction is not discussed here in detail. [Pg.148]

Ismail W, M El-Said Mohamed, BE Wanner, KA Datsenko, W Eisenreich, F Rohdich, A Bacher, G Fuchs (2003) Functional genomics by NMR spectroscopy. Phenylacetate catabolism in Escherichia coli. Eur JBiochem 270 3047-3054. [Pg.292]


See other pages where Escherichia coli function is mentioned: [Pg.6]    [Pg.6]    [Pg.315]    [Pg.300]    [Pg.97]    [Pg.129]    [Pg.142]    [Pg.154]    [Pg.112]    [Pg.338]    [Pg.396]    [Pg.247]    [Pg.434]    [Pg.548]    [Pg.1234]    [Pg.187]    [Pg.73]    [Pg.176]    [Pg.23]    [Pg.58]    [Pg.374]    [Pg.58]    [Pg.151]    [Pg.155]    [Pg.173]    [Pg.182]    [Pg.184]   
See also in sourсe #XX -- [ Pg.80 ]




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Escherichia coli, sequence-structure-function

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