Escherichia coli adenylate kinase

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. 

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. 

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. 

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). 

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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