Genetic and Functional Diversity of Nitrilases in Agaricomycotina
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F19%3A00519687" target="_blank" >RIV/61388971:_____/19:00519687 - isvavai.cz</a>
Result on the web
<a href="https://www.mdpi.com/1422-0067/20/23/5990" target="_blank" >https://www.mdpi.com/1422-0067/20/23/5990</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/ijms20235990" target="_blank" >10.3390/ijms20235990</a>
Alternative languages
Result language
angličtina
Original language name
Genetic and Functional Diversity of Nitrilases in Agaricomycotina
Original language description
Nitrilases participate in the nitrile metabolism in microbes and plants. They are widely used to produce carboxylic acids from nitriles. Nitrilases were described in bacteria, Ascomycota and plants. However, they remain unexplored in Basidiomycota. Yet more than 200 putative nitrilases are found in this division via GenBank. The majority of them occur in the subdivision Agaricomycotina. In this work, we analyzed their sequences and classified them into phylogenetic clades. Members of clade 1 (61 proteins) and 2 (25 proteins) are similar to plant nitrilases and nitrilases from Ascomycota, respectively, with sequence identities of around 50%. The searches also identified five putative cyanide hydratases (CynHs). Representatives of clade 1 and 2 (NitTv1 from Trametes versicolor and NitAg from Armillaria gallica, respectively) and a putative CynH (NitSh from Stereum hirsutum) were overproduced in Escherichia coli. The substrates of NitTv1 were fumaronitrile, 3-phenylpropionitrile, beta-cyano-l-alanine and 4-cyanopyridine, and those of NitSh were hydrogen cyanide (HCN), 2-cyanopyridine, fumaronitrile and benzonitrile. NitAg only exhibited activities for HCN and fumaronitrile. The substrate specificities of these nitrilases were largely in accordance with substrate docking in their homology models. The phylogenetic distribution of each type of nitrilase was determined for the first time.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10612 - Mycology
Result continuities
Project
<a href="/en/project/GA18-00184S" target="_blank" >GA18-00184S: New "nitrilase superfamily" proteins in Basidiomycota: study of their activities and potential functions in the biodegradation of cyanide and nitriles</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2019
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
International Journal of Molecular Sciences
ISSN
1422-0067
e-ISSN
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Volume of the periodical
20
Issue of the periodical within the volume
23
Country of publishing house
CH - SWITZERLAND
Number of pages
19
Pages from-to
5990
UT code for WoS article
000504428300172
EID of the result in the Scopus database
2-s2.0-85075716861