COMPARATIVE ANALYSIS OF LIPASES IN VIEW OF PROTEIN DESIGN
Abstract
The consensus sequences containing the active serine residue of 21 lipases were examined for structural properties by secondary structure prediction and hydrophobicity plots. Mostof the G-X-S-X-G peptides were found to form a turn structure andto be buried,i.e. inaccessible to water. The structural characters of a second serine containing consensus peptide describedin literature were compared to those of the G-X-S-X-G sequences. In addition, we investigated,if a correlation of the structural features of these peptides to the substrate specificity (regio specificity and fatty acid specificity) can be found.Citation
Lipases : structure, mechanism and genetic engineering, 421 - 424Affiliation
GBF, Gesellschaft fiir Biotechnologische Forschung mbH, Dept. of Enzyme Technology, Mascheroder Weg 1, D-3300 BraunschweigType
Book chapterconference paper
Language
enSeries/Report no.
GBF monographs ; Volume 16ISSN
0930-4320ISBN
156081165X3527283323
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