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COMPARATIVE ANALYSIS OF LIPASES IN VIEW OF PROTEIN DESIGN
Kordel, Marianne Menge, Ulrich Morelle, Gilles Erdmann, Helmut Schmid, Rolf D.
Kordel, Marianne
Menge, Ulrich
Morelle, Gilles
Erdmann, Helmut
Schmid, Rolf D.
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Issue Date
1991
Submitted date
2024-03-27
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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 - 424
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Book chapter
conference paper
conference paper
Language
en
Description
Series/Report no.
GBF monographs ; Volume 16
ISSN
0930-4320
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ISBN
156081165X
3527283323
3527283323
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Attribution-NonCommercial-ShareAlike 4.0 International