Sulfolobus solfataricus

Biochemical and biophysical aspects of hyperthermophilic enzymes are as wide-ranging as all correspondent aspects of mesophilic enzymes but also include specific peculiarities. In this section some specific features of one of the typical hyperthermophylic enzymes, p-glycosidase Sulfolobus solfataricus, will be considered. 

P-glycosidase from the hyperthermophylic archaeon Sulfolobus solfataricus and its recombinants appear to be convenient objects for studying the relationship between intramolecular dynamics and enzyme activity (Nucci et al., 1993 Moracci et al., 1996 D Auria et al., 1998, 1999 Bismuto et al., 1999). The enzyme is barely active up to 

showing its maximal activity above 95°C and thermostability with a t1/2 of 85 h at 75 °C. Using a special stainless steel optical pressure cell, enzyme assays and fluorescence measurements up to pressure of 160 atmosphere boiling the sample have been performed (D Auria et al., 1999). The enzyme showed maximal activity at 125 °C. 

An additional insight into the contribution of various interactions for protein stability and rigidity may be gained by a comparative data analysis of the differential scanning calorimetry (DSC) of the hyperthermostable and mesophilic enzymes. Accordingly, the 

The following peculiarities of the hyperthermostable P-glycosidase, which are different from that for proteins from mesophylic micro-organisms, were revealed in the results of the spin labelling experiments. 

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Cacciapuoti G, M Porcelli, M de Rosa, A Gambacorta, C Bertoldo, V Zappia (1991) 5 -adenosylmethionine decarboxylase from the thermophilic archaebacterium Sulfolobus solfataricus. Putification, molecular properties and studies on the covalently bound pyruvate. Eur J Biochem 199 395-400. 

Albers, S.V., Jonuscheit, M., Dinkelaker, S. et al. (2006) Production of recombinant and tagged proteins in the hyperthermophilic archaeon Sulfolobus solfataricus. Applied and Environmental Microbiology, 72 (1), 102-111. 

The transesterification of phenyl-/J-D-glucoside catalyzed by Sulfolobus solfataricus [81b] was quantitative within 2 h at 110 °C under the action of irradiation whereas the yield was only 60% after 40 h under classical conditions (Scheme 8.57). 

Durr H, Korner C, Muller M, Hickmann V, Hopfner KP (2005) X-ray structures of the Sulfolobus solfataricus SW12/SNF2 ATPase core and its complex with DNA. Cell 121 363-373 Eberharter A, Becker PB (2004) ATP-dependent nucleosome remodelling factors and functions. J Cell Sci 117 3707-3711... 

Amino-5 -deoxy-D-gluconohydroximo-1,5-lactam (124) H a-Glucosidase Sulfolobus solfataricus 1UWU 259... 

T. M. Gloster, S. Roberts, V. M-A Ducros, G. Perugino, M. Rossi, R. Hoos, M. Moracci, A Vasella, and G. J. Davies, Structural studies of the p-glucosidase from Sulfolobus solfataricus in complex with covalently and noncovalently bound inhibitors, Biochemistry, 43 (2004) 6101-6109. 

Different purified or partially purified enzymes were tested successfully, such as horse liver dehydrogenase [3], Sulfolobus solfataricus dehydrogenase [4], Pischia pastoris alcohol oxidase [5, 6], the baker s yeast alcohol dehydrogenase [7], and finally lipolytic enzymes, which probably constitute the major part of the work devoted to the use of enzymes working at the solid/gas interface, as summarized in a recent publication [8]. 

Cannio, R. Contursi, P. Rossi, M. Bartolucci, S. Thermoadaptation of a mesophilic hygromycin B phosphotransferase by directed evolution in hy-perthermophilic Archaea selection of a stable genetic marker for DNA transfer into Sulfolobus solfataricus. Extremophiles, 5, 153-159 (2001)... 

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)... 

Besides sponges and algae, enzymes were also isolated from marine organisms and microorganisms. For example, polymerases and proteases from marine Vibrio sp. [352], marine bacterium such as Alcaligenes faecalis [353], and from archaeons, such as the psychrophilic Cenarchaeum symbiosum [354], and the hyperthermophile archaeons Pyrococcus furiosus [355], Sulfolobus solfataricus [356], and Aeropyrum pernix [357] transferases from marine bacterium such as Vibrio vulnificus... 

Boudsocq, F., Iwai, S., Hanaoka, F., and Woodgate, R. (2001). Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4) An archaeal DNA polymerase with lesion-bypass properties akin to eukaryotic pol q. Nucleic Acids Res. 15, 4607-4613. 

A. Trincone, E. Pagnotta, M. Rossi, M. Mazzone, and M. Moracci, Enzymatic synthesis of 2-deoxy-P-glucosides and stereochemistry of P-glycosidase from Sulfolobus solfataricus on glucal, Tetrahedron Asymmetry, 12 (2001) 2783-2787. 

Sulfolobus solfataricus Thermophile Label-free Phosphoproteomics (219)... 

Cobucci-Ponzano, B., Trincone, A., Giordano, A., Rossi, M. and Moracci, M. (2003c). Identification of the catalytic nucleophile of the family 29 alpha-L-fucosidase from Sulfolobus solfataricus via chemical rescue of an inactive mutant. Biochemistry, 42, 9525-9531. 

Gloster, T.M., Roberts, S., Ducros, V.M., Perugino, G., Rossi, M., Hoos, R., Moracci, M., Vasella, A. and Davies, G.J. (2004) Structural studies of the beta-glycosidase from Sulfolobus solfataricus in complex with covalently and noncovalently bound inhibitors. 

Lower, B.H. and Kennelly, P.J. (2002) The membrane-associated protein-serine/threonine kinase from Sulfolobus solfataricus is a glycoprotein. J Bacteriol, 184, 2614-2619. 

Moracci, M., Capalbo, L., Ciaramella, M., and Rossi, M. (1996) Identification of two glutamic acid residues essential for catalysis in the p-glycosidase from the thermoacidophilic archaeon Sulfolobus solfataricus. Protein Eng. 12, 1191-1195. 

Moracci, M., Ciaramella, M., Nucci, R., Pearl, L.H., Sanderson, I., Trincone, A. and Rossi, M. (1994) Thermostable p-glycosidase from Sulfolobus solfataricus. Biocatalysis, 11, 89-103. 

Trincone, A., Nicolaus, B., Lama, L. and Gambacorta, A. (1991) Stereochemical studies of enzymatic transglycosylation using Sulfolobus solfataricus. J Chem Soc Perkin Trans, 1, 2841-2844... 

Park SY, Yamane K, Adachi S, et al. Thermophilic cytochrome P450 (CYP119) from Sulfolobus solfataricus high resolution structure and functional properties. J Inorg Biochem 2002 91 491-501. 

Chang YT, Loew G. Homology modeling, molecular dynamics simulations, and analysis of CYP119, a P450 enzyme from extreme acidothermophilic archaeon Sulfolobus solfataricus. Biochemistry 2000 39 2484—2498. 

A large number of hyperthermophilic Archaebacteria, especially the deep sea Thermococcale and Sulfolobus species elaborate a-amylases.79-82 Many have been cloned and sequenced.78 Pyrococcus furiosus,83,84 Thermococcus profundus,85 Thermococcus hydrothermalis,78 Sulfolobus solfataricus and Sulfolobus acidocaldar-iusS6 secrete thermophilic a-amylases. The a-amylases of all of these organisms have optimal enzyme activity at 90°C or higher and often only begin to show activity at 40°C or 50°C. Pyrococcus furiosus secretes an a-amylase with an optimum temperature of 100°C and a maximum temperature of 140°C.87 The optimum pH values vary between 5 and 9. Table 7.1 summarizes the names of the organisms, the optimum temperature, and optimum pH values for several of these enzymes. 

Halobacterium salinarium Methanosarcina frisia Sulfolobus acidocaldarius Sulfolobus solfataricus... 

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