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Crystallization and Preliminary X-ray Studies of Lipase from Geotrichum candidum
Menge, Ulrich Hecht, Hans-Jürgen Schomburg, Dietmar Schmid, Rolf D. Hedrich, H. C. Spener, F.
Menge, Ulrich
Hecht, Hans-Jürgen
Schomburg, Dietmar
Schmid, Rolf D.
Hedrich, H. C.
Spener, F.
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Issue Date
1991
Submitted date
2024-03-13
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Abstract
Wehave succeeded in the production of new crystals of lipase from Geotrichum candidum which were suitable for a refined X-ray analysis. First measurements proved the lattice constant and space group to be similar to that reported by Hata et al. /1/. However, these crystals can be analyzed without any cross-linking. This should enable a higher resolution for the structure determination of the lipase from Geotrichum candidum. Inhibition experiments with this lipase proved metal ions, iodine and p-chloromercuribenzoate to effect the enzyme activity. Metal ions inactivated lipase at a 1000-fold excess and in the order of Ag*>Hg’* >Co**>Zn**. In contrast, I, and p-chloromercuribenzoate modified lipase from Geotrichum candidum in stoichiometric amounts. These modified as well as a deglycosylated lipase could becrystallized. Such crystals ofslightly modified lipases offer the chance of analyzing further details of the lipase structure, e.g. the influence of the glycosylation on the tertiary structure, and they are an alternative approach to high quality crystals.
Citation
Lipases : structure, mechanism and genetic engineering, 59 - 62
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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