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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1993-3-2
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pubmed:databankReference |
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pubmed:abstractText |
A lipase gene (lip1) from the facultative psychrophilic strain Psychrobacter immobilis B10 has been cloned and sequenced. The deduced preprotein sequence is composed of 317 amino acids with a predicted M(r) of 35,288. A primary structure alignment of lipases including lip1 shows conserved elements for which a structural role is proposed in the light of recent crystallographic studies. The analysis of the psychrophilic enzyme sequence suggests characteristics in relation with the adaptation to cold.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0006-3002
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
1171
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
331-3
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
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pubmed:year |
1993
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pubmed:articleTitle |
Cloning, sequence and structural features of a lipase from the antarctic facultative psychrophile Psychrobacter immobilis B10.
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pubmed:affiliation |
Laboratoire de Biochimie, Université de Liège-Sart Tilman, Belgium.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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