Cloning, Sequence and Structural Features of a Lipase from the Antarctic Facultative Psychrophile Psychrobacter Immobilis B10

peer reviewed 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 conser...

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Bibliographic Details
Published in:Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression
Main Authors: Arpigny, J. L., Feller, Georges, Gerday, Charles
Format: Article in Journal/Newspaper
Language:English
Published: Elsevier 1993
Subjects:
Life sciences
Biochemistry
biophysics & molecular biology
Sciences du vivant
Biochimie
biophysique & biologie moléculaire
Antarc*
Antarctic
Online Access:https://orbi.uliege.be/handle/2268/16332
https://doi.org/10.1016/0167-4781(93)90078-R
Description
Summary:peer reviewed 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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