Escherichia coli adenylation

Saint Girons, I. Gilles, A.-M. Margarita, D. Michelson, S. Monnot, M. Fermandjian, S. Danchin, A. Barzu, O. Structural and catalytic characteristics of Escherichia coli adenylate kinase. J. Biol. Ghent., 262, 622-629 (1987)... 

Bilderback, T. Fulmer, T. Mantulin, W.W. Glaser, M. Substrate binding causes movement in the ATP binding domain of Escherichia coli adenylate kinase. Biochemistry, 35, 6100-6106 (1996)... 

Lin, Y. Nageswara Rao, B.D. Structural characterization of adenine nucleotides bound to Escherichia coli adenylate kinase. 2. P and C Relaxation measurements in the presence of cobalt(II) and manganese(ll). Biochemistry, 39, 3647-3655 (2000)... 

Ratner, V., Kahana, E., and Haas, E.. (2002), The natively helical chain segment 169-188 of Escherichia coli adenylate kinase is formed in the latest phase of the refolding transition, J. Mol.. Biol. 320, 1135-1145. 

Y.E. Shapiro, E. Kahana, V. Tugarinov, Z. Liang, J.H. Freed, E. Meirovitch, Domain flexibility in hgand-free and inhibitor-bound Escherichia coli adenylate kinase based on a mode-conphng analysis of N spin-relaxation. Biochemistry 41 (2002) 6271-6281. 

Knowledge of the coenzyme forms of vitamin Bi2 has increased steadily. The first coenzyme of Bi2 isolated from bacteria had similarities to pseudovitamin Bi2 it contained adenylic acid instead of 5,6-dimethyl-benzimidazole, but differed in lacking cyanide and having an extra molecule of adenine which was assumed to be bound to the cobalt atom by the coordination site, often occupied by cyanide (B24). This coenzyme, adenylcobamide, was completely inactive for Ochromonas malhamensis, but active for Escherichia coli 113-3. 

Okajima, T. Kitaguchi, D. Fujii, K. Matsuoka, H. Goto, S. Uchiyama, S. Kobayashi, Y Tanizawa, K. Novel trimeric adenylate kinase from an extremely thermoacidophilic archaeon, Sulfolobus solfataricus molecular cloning, nucleotide sequencing, expression in Escherichia coli, and characterization of the recombinant enzyme. Biosci. Biotechnol. Biochem., 66, 2112-2124 (2002)... 

K. Ishige and T. Noguchi (2000). Inorganic polyphosphate kinase and adenylate kinase participate in the polyphosphate AMP phosphotransferase activity of Escherichia coli. Proc. Natl. Acad. Sci. USA, 976, 14168-14171. 

Similar substances containing adenylic acid and amino acids have been obtained from Escherichia coli and from Bacillus subtilisP... 

In diseases of the small intestine, active secretion caused by cyclic nucleotide stimulation can result in a large volume of water and electrolytes moving into the lumen. Additionally, enteric neuron activation of mast cells can increase intestinal capillary permeability and promote passive fluid secretion. Diseases that increase intestinal permeability can result in passive secretion of protein-rich fluid into the intestinal lumen. Active secretion of electrolytes and water is a feature of many diarrheal disorders and can be stimulated by bacterial enterotoxins. Several bacterial enterotoxins interact with intestinal epithelial cell membrane adenylate cyclase or guanylate cyclase, resulting in increased cAMP or cGMP. These, in turn, activate basolateral chloride channels, resulting in an increase in the luminal secretion of chloride, accompanied by sodium and followed by water (Gemmell 1984). Bacterial enterotoxins that stimulate cAMP include cholera toxin, Escherichia coli... 

Graziano MP, Casey PJ, Gilman AG (1987) Expression of cDNAs for G proteins in Escherichia coli Two forms of Gso sfimulate adenylate cyclase. In J. Biol. Chem. 262 11375-11381. 

Crepin, T., Schmitt, E., Mechulam, Y., et al. (2003) Use of analogues of methionine and methio-nyl adenylate to sample conformational changes during catalysis in Escherichia coli methionyl-tRNA synthetase. J. Mol. Biol., 332(1), 59-72. 

In a separate pathway, MTP synthase is regenerated (grouped within a grey box in Fig. 4.12) by transferring sulfur to the small subunit. In Escherichia coli, MoeB catalyses the adenylation of the carboxyl of the C-terminal Gly residue of MoaD, in a reaction very similar to that catalysed by the El enzyme that activates ubiquitin in the ubiquitin/proteasome pathway referred to earlier. The AMP-activated MoaD is then sulfurated by sulfide transfer from an unknown donor. It is assumed that Cu is inserted directly after dithiolate formation. In the last two steps, adenylated MPT is formed from Mg-ATP, and, finally, in the presence of molybdate (MoOa ), bound MPT-AMP is hydrolysed, Cu is released and Mo is transferred to the MPT dithiolate, and the MoCo cofactor is released. 

Chapman, A.G., Fall, L. and Atkinson, D.E., 1971. Adenylate energy in Escherichia coli during growth and starvation. J. Bacteriol., 108 1072—1086. 

Muller CW, Schulz GE. Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state. J Mol Biol 1992 224(1) 159-177. 

Purification of 6-phosphogluconate dehydrogenase from Escherichia coli Purification of adenylate cyclase... 

Escherichia coli heat-lahile entero toxin Nucleotide-hinding component of adenylate cyclase 74, 141, 142... 

ADP-Ribosylation of human c-Ha-ras protein by hen liver ADP-ribosyl transferase. Human c-Ha-ras protein, normal or mutated from glycine to valine at the 12th position, was produced in Escherichia coli and purified (6). These proteins were incubated with ADP-ribosyl transferase purified from hen liver nuclei (7) in the presence of [adenylate- P]NAD. Incorporation of the radioactivity derived from p PJNAD was clearly shown at the positions corresponding to the protein bands of normal and mutated c-Ha-m.y proteins (Fig. lA and IB, lanes 3 and 4). However no significant radioactive band was formed in the absence of c-Ha-ra proteins (Fig. IB, lane 5). The incorporation of the radioactivity into c-Ha-ra.y protein was inhibited by more than 50% in the presence of 40 mM arginine methylester or 40 mM nicotinamide. 

Guanylate kinase has been partly purified from hog brain 10), from Escherichia coli 11), and from a transplantable mouse tumor, Sarcoma 180 12). These preparations show similarities with respect to substrate specificity and cation requirements, but differ with respect to pH optima and molecular weight. All three preparations are highly specific in that guanylate and deoxyguanylate are phosphorylated, but adenylate, ino-sinate, xanthylate, and cytidylate are not substrates. The brain and tumor enzymes also phosphorylate 8-azaguanylate. ATP or dATP are the specific phosphate donors for the three enzymes. 

Thiamine is metabolized to TPP by thiamine pyrophosphokinase (EC 2.1.62) in animal cells including red and white blood cells. This enzyme is also present in plants, yeast, and a bacterium (Paracoccus denitrificans) (7). However, in some bacteria, for example in Escherichia coli, thiamine is metabolized to TPP by a two-step reaction catalyzed by thiamine kinase (EC 2.7.1.89) and TMP kinase (EC 2.7.4.10). Thiamine pyrophosphate is further metabolized to TI P in yeast, animal tissues, and human red blood cells. Evidence has been obtained which indicates that cytosolic adenylate kinase (EC 2.7.4.3) catalyzes TIP synthesis from TPP in vitro (8) and in vivo (3). The enzyme system involved in thiamine metabolism to TTP in human red blood cells was recently identified, purified, and reconstituted (9). 

Hewlett, E. L., Guerrant, R. L., Evans, D. J., and Greenough, W. B., 1974, Toxins of Vibrio cholerae and Escherichia coli stimulate adenyl cyclase in rat fat cells. Nature 249 371. 

The adenylate kinases from the three bacteria studied were found to be heat-labile. Enzymes revealing similar behavior were described for rat liver (Sapico et al., 1972), baker s yeast (Chiu et al., 1967), Escherichia coli (Holmes and Singer, 1973), Pseudomonas denitrificans (Terai, 1974) and from spinach chloroplast evelopes (Murakami and Strotmann, 1978). On the other hand, the adenylate kinase from muscle or beef heart mitochondria were reported to be heat-stable (Albrecht, 1970 Colowick and Kalckar, 1943). 

Holmes RK, Singer MF (1973) Purification and characterization of adenylate kinase as an apparent adenosine triphosphate dependent inhibitor of ribonuclease II in Escherichia coli, J. Biol. Chem. 248, 2014-2021. 

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