Expression and characterization of plant aspartic protease nepenthesin-1 from Nepenthes gracilis
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F14%3A10191762" target="_blank" >RIV/00216208:11310/14:10191762 - isvavai.cz</a>
Alternative codes found
RIV/61388971:_____/14:00428463
Result on the web
<a href="http://dx.doi.org/10.1016/j.pep.2013.12.005" target="_blank" >http://dx.doi.org/10.1016/j.pep.2013.12.005</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.pep.2013.12.005" target="_blank" >10.1016/j.pep.2013.12.005</a>
Alternative languages
Result language
angličtina
Original language name
Expression and characterization of plant aspartic protease nepenthesin-1 from Nepenthes gracilis
Original language description
Carnivorous plants of the genus Nepenthes produce their own aspartic proteases, nepenthesins, to digest prey trapped in their pitchers. Nepenthesins differ significantly in sequence from other aspartic proteases in the animal or even plant kingdoms. Thisdifference, which also brings more cysteine residues into the structure of these proteases, can be a cause of uniquely high temperature and pH stabilities of nepenthesins. Their detailed structure characterization, however, has not previously been possible due to low amounts of protease present in the pitcher fluid and also due to limited accessibility of Nepenthes plants. In the present study we describe a convenient way for obtaining high amounts of nepenthesin-1 from Nepenthes gracilis using heterologous production in Escherichia coli. The protein can be easily refolded in vitro and its characteristics are very close to those described for a natural enzyme isolated from the pitcher fluid. Similarly to the natural enzyme, recombinant
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Protein Expression and Purification
ISSN
1046-5928
e-ISSN
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Volume of the periodical
95
Issue of the periodical within the volume
March 2014
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
8
Pages from-to
121-128
UT code for WoS article
000332192900017
EID of the result in the Scopus database
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