Source:http://linkedlifedata.com/resource/pubmed/id/19508183
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
2009-10-28
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pubmed:abstractText |
Thermophilic and hyperthermophilic carboxylesterases (EC 3.1.1.1) are excellent model systems for studying structure function relationships as well as in vitro and in vivo evolution and possible biotechnological applications. In this paper we review the main aspect of one of most studied microbial representative of the hormone sensitive lipase family (HSL), namely carboxylesterase 2 (EST2) from Alicyclobacillus acidocaldarius.
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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:issn |
1875-5305
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1189-200
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pubmed:meshHeading |
pubmed-meshheading:19508183-Alicyclobacillus,
pubmed-meshheading:19508183-Bacterial Proteins,
pubmed-meshheading:19508183-Carboxylesterase,
pubmed-meshheading:19508183-Catalytic Domain,
pubmed-meshheading:19508183-Kinetics,
pubmed-meshheading:19508183-Mutation,
pubmed-meshheading:19508183-Protein Structure, Secondary,
pubmed-meshheading:19508183-Protein Structure, Tertiary,
pubmed-meshheading:19508183-Sterol Esterase,
pubmed-meshheading:19508183-Substrate Specificity
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pubmed:year |
2009
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pubmed:articleTitle |
Structural and kinetic overview of the carboxylesterase EST2 from alicyclobacillus acidocaldarius: a comparison with the other members of the HSL family.
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pubmed:affiliation |
Institute of Protein Biochemistry (IBP), National Research Council (CNR), Via Pietro Castellino 111, 80131, Naples, Italy.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Review
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