Enzyme sulfolobus solfataricus

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]. 

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... 

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. 

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... 

D Auria, S., Nucci, R., Rossi, M., Gryczynski, I., Gryczynski, Z., and Lakowicz, J. R. (1999) The (3-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus enzyme activity and conformational dynamics at temperatures above 100°C, Biophys. Chem. 81, 23-31. 

The unknotting reaction (typical of type II DNA topoisomerases) is ten times more efficient than relaxation. The most purified fraction contained two major polypeptides of 40 and 60 kDa. The S. acidocaldarius type II DNA topoisomerase has no DNA gyrase activity. This suggested that it could specifically resemble the eukaryotic type II DNA topoisomerase however, taking into account its putative dimeric structure, it could also resemble the new type II DNA topoisomerase (topo IV) recently discovered in E. co/i [70]. We have recently detected in our laboratory a type II DNA topoisomerase in Sulfolobus shibatae. This enzyme catalyzes the same reactions as the enzyme from Sulfolobus solfataricus and exhibits a pattern of drug sensitivity very similar to that of the eukaryotic enzyme [Bergerat, A., this laboratory]. 

Archaeal chromosomes have been shown to be circular in three cases. For Thermococcus celer [12], restriction mapping of the entire chromosome with three rare-cutting enzymes clearly demonstrated circularity. Sulfolobus solfataricus DNA gives two... 

The target range of the archaeal Type II chaperonins remains to be investigated. No natural in vivo targets have been identified to date, although there are reports of facilitated folding in vitro of several thermophilic enzymes by the thermosomes from Sulfolobus solfataricus (Guagliardi et al., 1994) and Methanococcus thermolithotrophicus (Furutani etal., 1998). 

A NAD+ dependent ADH isolated from Sulfolobus solfataricus was found to exhibit better thermostability than HLADH [t /2 (60 °C) = 20 h] together with a distinctive preference for (S)-alcohols (complementary to HLADH)[861. The enzyme has a broad substrate specificity that includes linear and branched primary alcohols and linear and cyclic secondary alcohols1481. The highly purified enzyme exhibits a specific activity of 4 U mg-1 (for benzyl alcohol at 65 °C)187, 881. To date, this enzyme is not commercially available. 

In this connection, crystal structures of the (+) - trans-anti-1 i a P D E- N2-dG adduct in the Y-family lesion bypass DNA polymerase IV (Dpo4) (see also Chapter 15 by Chandani and Loechler) from the archaeon Sulfolobus solfataricus reveal that the favored P domain is preserved in the enzyme in this case [51], Overall, a survey of crystal structures of DNA damaged by polycyclic carcinogenic chemicals shows that structures observed in DNA duplexes in solution by high-resolution NMR methods are often observed in polymerases [37] however, the preferred P domain can be overridden by strong lesion-polymerase interactions, as was manifested in a crystal structure of a B[a]PDE-derived adenine lesion [52],... 

A., Atomi, H., and Nidetzky, B. (2009) Short-chain a-l,4-glucan phospho-rylase having a truncated N-terminal domain functional expression and characterization of the enzyme from Sulfolobus solfataricus. Biochim. Bio-phys. Acta, 1794, 1709-1714. 

Many enzymes have been isolated and characterized from Sulfolobus solfataricus. All are thermophilic, thermostable and show resistance to denaturating agents and organic solvents (6-11). In this work we present prelimiruuy results on an ADP-ribosyl transferase activity in Sulfolobus solfataricus. 

In conclusion, these results indicate that Sulfolobus solfataricus ceU-free system contains a significant ADP-ribosyl transferase activity. It seems of relevant interest that this archaebacterium is the most primitive organism in which ADP-ribosylation has been demonstrated. Furthermore the enzymatic activity appears to be thermophilic, a unique property never observed for the same kind of enzyme isolated from other sources (17). Further studies are in progress on the purification and characterization of the enzyme to investigate its biological role. As mentioned above, several biochemical properties demonstrated that sulfur-dependent archaebacteria are closer related to eukaryotes than to eubacteria (3). These findings support the hypothesis that the ADP-ribosyl transferase activity which we found associated primarily with the nucleoprotein fraction of Sulfolobus solfataricus, could play a role in any cellular event in which the enzyme is known to be involved in eukaryotic cells (17). 

Malic enzyme has been isolated from the archaebacterium Sulfolobus solfataricus and has been shown to be essentially NADP" dependent and is markedly thermostable [132]. It was activated by NH, but there was no absolute requirement for the ion and its presence decreased the affinity of the enzyme for both malate and NADP [132]. The high resistance of the enzyme to organic solvents and general protein denaturants has been studied in some detail [133]. Typically the... 

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