Escherichia coli relationship

Holms, W.H. (1986) The central metabolic pathways of Escherichia coli relationship between flux and control at a branch point, efficiency of conversion to biomass, and excretion of acetate. Curr. Top. Cell. Regul 28, 69-106. 

Bortolussi, R., Ferrieri, R, Bjorksten, B., and Quie, P. G., 1979, Capsular K1 polysaccharide of Escherichia coli Relationship to virulence in newborn rats and resistance to phagocytosis. Infect. Immun. 25 293-298. 

Tsou AY, SC Ransom, JA Gerlt, DD Buechter, PC Babbitt, GL Kenyon (1990) Mandelate pathway of Pseudomonas putida sequence relationships involving mandelate racemase, (5)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli. Biochemistry 29 9856-9862. 

The synthesis and antibacterial properties of norfloxacin (2a) were described in 1980 [65]. In this key paper in the evolution of quinolone antibacterial agents, a series of 6,7,8-polysubstituted-l-ethyl-l,4-dihydro-4-oxoquinoline-3-carb-oxylic acids (13) was synthesized, employing previously developed quantitative structure-activity relationships (QSAR) for the corresponding 6-, 7- and 8-monosubstituted derivatives versus Escherichia coli. The QSAR analysis... 

Cohen, P. S., Rossoll, R., Cabelli, V. J., Yang, S. L., and Laux, D. C. (1983). Relationship between the mouse-colonizing ability of a human fecal Escherichia coli strain and its ability to bind a specific mouse colonic mucous gel protein. Infect. Immun. 40,62-69. 

J.P. Richard, J.G. Westerfeld, S. Lin, Structure-reactivity relationships for beta-galactosidase (Escherichia coli, lac Z). 1. Bronsted parameters for cleavage of alkyl beta-D-galactopyranosides, Biochemistry 34 (1995) 11703-11712. 

Schneider, D. A., and Course, R. L. (2004) Relationship between growth rate and ATP concentration in Escherichia coli a bioassay for available cellular ATP. J Biol Chem. 279, 8262-8268. 

Escherichia coli have also developed an elegant method to control enzyme catalysis that occurs by covalent modification of each subunit. In this latter reaction a single tyrosyl residue per subunit is adenylylated to produce a stable 5 -adenylyl-O-tyrosyl derivative. Recent NMR and fluorescence data will be reviewed concerning the nature of this adenylyl site and its spatial relationship to the metal ions at the catalytic site. The enzymes responsible for the covalent adenylylation reaction comprise a cascade system for amplifying the activation or inactivation of glutamine synthetase molecules (81). 

Hall et al. (1960) reported on the relationship between electron density on the ring of substituted tryptophan and the rate of metabolism by Escherichia coli. 

Morozov II, Myasnik MN (1980) The relationship between the phenomenon of photoreactivation in Escherichia coli following ionizing radiation and Cerenkov emission. Radiat Res 82 336-341 Moss SH, Smith KC (1980) Cerenkov ultraviolet radiation (137Cs y-rays) and direct excitation (137Cs y-rays and 50 kVp X-rays) produce photoreactivable damage in Escherichia coli. Int J Radiat Biol 38 323-334... 

ECB deacylase is an 81-83-kDa heterodimer consisting of 63- and 18-20-kDa subunits. Penicillin G acylase from Escherichia coli is an 87-kDa heterodimer with 65- and 22-kDa subunits [32], For comparison, cephalosporin acylase from a Pseudomonas strain is an 83-kDa heterodimer consisting of 57- and 26-kDa subunits [33], The essential absence of any external catalytic requirement, cofactor stimulation, or product inhibition of ECB deacylase is also an intrinsic property of penicillin acylase [34], Based on the amino-terminal sequences of the two subunits of ECB deacylase, a 48% sequence similarity has been observed between the small subunit of ECB deacylase and a penicillin acylase [25]. This statistically significant albeit moderate sequence similarity from two short segments of the enzymes suggests an evolutionary relationship between ECB deacylase and peni-... 

A Sugino, CL Peebles, KN Kreuzer, NR Cozzarelli. Mechanism of action of nalidixic acid purification of Escherichia coli nalA gene product and its relationship to DNA gyrase and a novel nicking-closing enzyme. Proc Natl Acad Sci (USA) 74 4767-4771, 1977. 

However, some of the studies were limited by using 2,3,7,8-TCDD concentrations in excess of its solubility in water. Only two early studies reported positive results (Hussain et al. 1972 Seiler 1973). However, the results were limited by failure to demonstrate a dose-response relationship and by low bacterial survival rates. In addition, 2,3,7,8-TCDD exposure induced reverse mutations in Escherichia coli (Hussain et al. 1972) and in Saccharomyces cerevisiae (Bronzetti et al. 1983). The conflicting data obtained in the above studies may result from technical difficulties in testing 2,3,7,8-TCDD rather than from a lack of biological activity. Testing difficulties arise from an extreme insolubility of this compound and a high toxicity observed in some test systems, which would be anticipated to result in a very narrow window for effective genotoxic doses. 

Samuel, G., Hogbin, J.P., Wang, L., Reeves, P.R. Relationships of the Escherichia coli 0157, Olll, and 055 O-antigen gene clusters with those of Salmonella enterica and Citrobacter freundii, which express identical O antigens. J Bacteriol 186 (2004) 6536-6543. 

In this experiment we will examine some of the properties of the aspartate transcarbamylase of Escherichia coli, which is typical of many enzymes subject to feedback inhibition and which has been studied extensively. Aspartate transcarbamylase (ATCase) catalyzes the first reaction unique to the biosynthesis of pyrimidine nucleotides. ATCase is subject to specific inhibition by quite low concentrations of one of its end products, cytidine 5 -triphosphate (CTP). This relationship and two other regulatory interactions important to the control of pyrimidine biosynthesis are summarized in Figure 9-1. 

A substance later shown to be muramic acid (see Section IV,6) was clearly different from the product of Vi antigen, and, although the strain used in some of the Vi studies (Escherichia coli 5396/38) is one in which sialic acid has been detected, the properties of the Vi antigen are markedly different from the neuraminic acid pol3oner. Infrared spectra recorded for crystalline V-acetyl-neuraminic acid exhibit full detail and cannot be compared with that published for aminohexuronic acid, but that of the amorphous neuraminic acid polymer (colominic acid) is rather similar to that of the Vi antigen polymeric unit, since their functional groups are very similar. The relationship of these substances to the property of 0 -inagglutinability is discussed later (see p. 336). 

CopA of En. hirae could be expressed in Escherichia coli and purified to homogeneity by Ni-NTA affinity chromatography by means of an added histidine tag (Wunderh-Ye and Solioz, in press). Purified CopA has a pH optimum of 6.3 and a for ATP of 0.2 mM. The enzyme forms an acylphosphate intermediate, which is a hallmark of P- and CPx-type ATPases (Pedersen and Carafoh, 1987b). Purified CopA can now serve in the analysis of mechanistic aspects of copper transport and in the characterization of structure-function relationships. 

Figure 2 shows the relationships that link together the genome and the proteome. For clarity, many related objects are omitted from Figs. 1 and 2, such as the many other Escherichia coli genes that are components of its chromosome, the other reactions that are components of TRYPSYN-PWY, and the reactants and products of RXNO-2382. 

Carpousis AJ. The Escherichia coli RNA degradosome structure, function and relationship to other ribonucleolytic multienyzme complexes. Biochem. Soc. Trans. 2002 30 150-155. 

It should be noted that some anaerobic eubacteria (e.g. Escherichia coli, Clostridium acidurici, Chlorobium limicold) possess 2-oxoacid oxidoreductases, either in addition to, or instead of, the dehydrogenase complexes (ref. [37] and references therein). As in the archaebacteria, electrons are transferred to ferredoxin or flavodoxin and the enzymes are small oligomeric proteins. The evolutionary relationships of these enzymes converting pyruvate to acetyl-CoA will be discussed in section 6.2. 

Figure 3 Relationship between specimen temperature and ambient temperature during freeze-drying of aqueous suspension of Escherichia coli cells. (From Ref. 23.)...

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