Crystallization and preliminary X-ray crystallographic analysis of beta-D-mannosidase from Asperigillus niger
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F12%3A00058227" target="_blank" >RIV/00216224:14740/12:00058227 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Crystallization and preliminary X-ray crystallographic analysis of beta-D-mannosidase from Asperigillus niger
Original language description
Mannosidases are important enzymes involved in the glycosidic bond hydrolysis and cleavage of beta-D-mannose from oligomeric saccharides. Fungal beta-D-mannosidase was crystallized in the presence of D-mannose and iodine compound. Diffraction data were collected at HZB-BESSY on beamline 14.1. Detailed structural information will help to understand its functional role and the conformational behaviour of the substrate in the retaining glycosylhydrolase mechanism.
Czech name
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Czech description
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Classification
Type
O - Miscellaneous
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
<a href="/en/project/GAP207%2F10%2F0321" target="_blank" >GAP207/10/0321: The ways to N-acetyl-mannosamine structures via mannoside metabolizing enzymes</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2012
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů