Molecular and biochemical characterization of the recombinant amidase from hyperthermophilic archaeon Sulfolobus solfataricus

Extremophiles ◽  
2001 ◽  
Vol 5 (3) ◽  
pp. 183-192 ◽  
Author(s):  
Anna d' Abusco ◽  
Sergio Ammendola ◽  
Roberto Scandurra ◽  
Laura Politi
Keyword(s):  
Biochemical Characterization ◽  
Sulfolobus Solfataricus ◽  
Hyperthermophilic Archaeon

scholarly journals Genetic and biochemical characterization of a short-chain alcohol dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosu s

2001 ◽  
Vol 268 (10) ◽  
pp. 3062-3068 ◽  
Author(s):  
John van der Oost ◽  
Wilfried G. B. Voorhorst ◽  
Servé W. M. Kengen ◽  
Ans C. M. Geerling ◽  
Vincent Wittenhorst ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Biochemical Characterization ◽  
Short Chain ◽  
Chain Alcohol ◽  
Hyperthermophilic Archaeon ◽  
Short Chain Alcohol

scholarly journals Characterization of native and reconstituted exosome complexes from the hyperthermophilic archaeon Sulfolobus solfataricus

2006 ◽  
Vol 62 (4) ◽  
pp. 1076-1089 ◽  
Author(s):  
Pamela Walter ◽  
Franziska Klein ◽  
Esben Lorentzen ◽  
Anne Ilchmann ◽  
Gabriele Klug ◽  
...  
Keyword(s):  
Sulfolobus Solfataricus ◽  
Hyperthermophilic Archaeon

scholarly journals Identification and Characterization of Small RNAs in the Hyperthermophilic Archaeon Sulfolobus solfataricus

PLoS ONE ◽  
2012 ◽  
Vol 7 (4) ◽  
pp. e35306 ◽  
Author(s):  
Ning Xu ◽  
Yan Li ◽  
Ying-Tao Zhao ◽  
Li Guo ◽  
Yuan-Yuan Fang ◽  
...  
Keyword(s):  
Small Rnas ◽  
Sulfolobus Solfataricus ◽  
Hyperthermophilic Archaeon ◽  
Identification And Characterization

Biochemical characterization of deblocking aminopeptidase from hyperthermophilic archaeon Thermococcus onnurineus NA1

2007 ◽  
Vol 104 (3) ◽  
pp. 188-194 ◽  
Author(s):  
Hyun Sook Lee ◽  
Yona Cho ◽  
Yun Jae Kim ◽  
Kwanghyun Nam ◽  
Jung-Hyun Lee ◽  
...  
Keyword(s):  
Biochemical Characterization ◽  
Thermococcus Onnurineus Na1 ◽  
Hyperthermophilic Archaeon

scholarly journals Purification and biochemical characterization of a poly(ADP-ribose) polymerase-like enzyme from the thermophilic archaeon Sulfolobus solfataricus

1998 ◽  
Vol 335 (2) ◽  
pp. 441-447 ◽  
Author(s):  
Maria Rosaria FARAONE-MENNELLA ◽  
Agata GAMBACORTA ◽  
Barbara NICOLAUS ◽  
Benedetta FARINA
Keyword(s):  
Biochemical Characterization ◽  
Sulfolobus Solfataricus ◽  
Enzymic Activity ◽  
Sds Page ◽  
Thermophilic Archaeon ◽  
Displacement Assay ◽  
Elongation Step ◽  
Ph Range ◽  
Good Agreement

A poly(ADP-ribose) polymerase-like enzyme, detected in a crude homogenate from Sulfolobus solfataricus by means of activity and immunoblot analyses, was purified to electrophoretic homogeneity by a rapid procedure including two sequential affinity chromatographies, on NAD+-agarose and DNA-Sepharose. The latter column selected specifically the poly(ADP-ribosyl)ating enzyme with a 17% recovery of enzymic activity and a purification of more than 15000-fold. The molecular mass (54–55 kDa) assessed by SDS/PAGE and immunoblot was definitely lower than that determined for the corresponding eukaryotic protein. The enzyme was proved to be thermophilic, with a temperature optimum of approx. 80 °C, and thermostable, with a half-life of 204 min at 80 °C, in good agreement with the requirements of a thermozyme. It displayed a Km towards NAD+ of 154±50 µM; in the pH range 6.5–10.0 the activity values were similar, not showing a real optimum pH. The enzyme was able to bind homologous DNA, as evidenced by the ethidium bromide displacement assay. The product of the ADP-ribosylating reaction co-migrated with the short oligomers of ADP-ribose (less than 6 residues) from a eukaryotic source. Reverse-phase HPLC analysis of the products, after digestion with phosphodiesterase I, gave an elution profile reproducing that obtained by the enzymic digestion of the rat testis poly(ADP-ribose). These results strongly suggest that the activities of the purified enzyme include the elongation step.

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