Source:http://linkedlifedata.com/resource/pubmed/id/19121283
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
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| pubmed:dateCreated |
2009-2-19
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| pubmed:abstractText |
We report the biochemical and structural characterization of the purine-specific ribonucleoside hydrolase from the archaeon Sulfolobus solfataricus (SsIAG-NH). SsIAG-NH is a homodimer of 70kDa specific for adenosine, guanosine and inosine. SsIAG-NH is highly thermophilic and is characterized by extreme thermodynamic stability (T(m), 107 degrees C), kinetic stability and remarkable resistance to guanidinium chloride-induced unfolding. A disulfide bond that, on the basis of SDS-PAGE is positioned intersubunits, plays an important role in thermal stability. SsIAG-NH shares 43% sequence identity with the homologous pyrimidine-specific nucleoside hydrolase from S. solfataricus (SsCU-NH). The comparative sequence alignment of SsIAG-NH, SsCU-NH, purine non-specific nucleoside hydrolase from Crithidia fasciculata and purine-specific nucleoside hydrolase from Trypanosoma vivax shows that, only few changes in the base pocket are responsible for different substrate specificity of two S. solfataricus enzymes. The structure of SsIAG-NH predicted by homology modeling allows us to infer the role of specific residues in substrate specificity and thermostability.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Mar
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| pubmed:issn |
1096-0384
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:day |
1
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| pubmed:volume |
483
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
55-65
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| pubmed:meshHeading |
pubmed-meshheading:19121283-Amino Acid Sequence,
pubmed-meshheading:19121283-Animals,
pubmed-meshheading:19121283-Base Sequence,
pubmed-meshheading:19121283-Catalytic Domain,
pubmed-meshheading:19121283-Cloning, Molecular,
pubmed-meshheading:19121283-DNA Primers,
pubmed-meshheading:19121283-Enzyme Stability,
pubmed-meshheading:19121283-Genes, Archaeal,
pubmed-meshheading:19121283-Kinetics,
pubmed-meshheading:19121283-Models, Molecular,
pubmed-meshheading:19121283-Molecular Sequence Data,
pubmed-meshheading:19121283-N-Glycosyl Hydrolases,
pubmed-meshheading:19121283-Purine Nucleosides,
pubmed-meshheading:19121283-Recombinant Proteins,
pubmed-meshheading:19121283-Sequence Homology, Amino Acid,
pubmed-meshheading:19121283-Substrate Specificity,
pubmed-meshheading:19121283-Sulfolobus solfataricus,
pubmed-meshheading:19121283-Thermodynamics
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| pubmed:year |
2009
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| pubmed:articleTitle |
Biochemical characterization and homology modeling of a purine-specific ribonucleoside hydrolase from the archaeon Sulfolobus solfataricus: insights into mechanisms of protein stabilization.
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| pubmed:affiliation |
Dipartimento di Biochimica e Biofisica "F. Cedrangolo", Seconda Università di Napoli, Italy. marina.porcelli@unina2.it
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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