Nitrile-Converting Enzymes and their Synthetic Applications
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F16%3A00465386" target="_blank" >RIV/61388971:_____/16:00465386 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1002/9781118828083.ch12" target="_blank" >http://dx.doi.org/10.1002/9781118828083.ch12</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/9781118828083.ch12" target="_blank" >10.1002/9781118828083.ch12</a>
Alternative languages
Result language
angličtina
Original language name
Nitrile-Converting Enzymes and their Synthetic Applications
Original language description
The enzymatic hydrolysis of nitriles proceeds via two different pathways: a two step pathway catalyzed by nitrile hydratase and amidase, and a single‐step pathway catalyzed by nitrilase. Nitrile hydratase and nitrilase belong to different protein superfamilies, and their phylogenetic distribution is also different (nitrilases in plants, fungi, and bacteria but nitrile hydratases almost exclusively in bacteria). Nitrilases (EC 3.5.5.‐.) belong to the nitrilase superfamily, that is, nonpeptide C-N hydrolases with a Glu‐Lys‐Cys catalytic triad, and nitrile hydratasesn(4.2.1.84) are metalloenzymes containing a ferric or a cobalt (III) ion in their catalytic site. Due to their ability to transform an immense number of man‐made nitriles, the nitrile‐converting enzymes have found widespread use in synthetic organic chemistry. The advantages of enzymatic processes reside in their mild conditions, high yields, and high purities of the products and in their regio‐ or enantioselectivities.n
Czech name
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Czech description
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Classification
Type
C - Chapter in a specialist book
CEP classification
EE - Microbiology, virology
OECD FORD branch
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Result continuities
Project
<a href="/en/project/GAP504%2F11%2F0394" target="_blank" >GAP504/11/0394: Interspecies comparison of nitrilases by using recombinant enzymes obtained by database-mining: their environmental impact and potential application</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Book/collection name
Green Biocatalysis
ISBN
9781118822296
Number of pages of the result
19
Pages from-to
331-350
Number of pages of the book
762
Publisher name
John Wiley & Sons
Place of publication
Hoboken, New Jersey
UT code for WoS chapter
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