Resolution of alpha/beta-amino acids by enantioselective penicillin G acylase from Achromobacter sp.
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F15%3A10297850" target="_blank" >RIV/00216208:11310/15:10297850 - isvavai.cz</a>
Alternative codes found
RIV/61388971:_____/15:00455568 RIV/00216224:14310/15:00085553
Result on the web
<a href="http://dx.doi.org/10.1016/j.molcatb.2015.09.008" target="_blank" >http://dx.doi.org/10.1016/j.molcatb.2015.09.008</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.molcatb.2015.09.008" target="_blank" >10.1016/j.molcatb.2015.09.008</a>
Alternative languages
Result language
angličtina
Original language name
Resolution of alpha/beta-amino acids by enantioselective penicillin G acylase from Achromobacter sp.
Original language description
Penicillin G acylases (PGAs) are enantioselective enzymes catalyzing a hydrolysis of stable amide bond in a broad spectrum of substrates. Among them, derivatives of ?MINUS SIGN and ?-amino acids represent a class of compounds with high application potential. PGAEc from Escherichia coli and PGAA from Achromobacter sp. CCM 4824 were used to catalyze enantioselective hydrolyses of seven selected N-phenylacetylated ?/#X?S#?et?;-amino acid racemates. The PGAA showed higher stereoselectivity for three enantiomers of N-PhAc-?-homoleucine, N-PhAc-?-tert-leucine and N-PhAc-?-leucine. To study the mechanism of enantiodiscrimination on molecular level, we have constructed a homology model of PGAA that was used in molecular docking experiments with the same substrates. In-silico experiments successfully reproduced the data from experimental enzymatic resolutions confirming validity of employed modeling protocol. We employed this protocol to evaluate enantiopreference of PGAA towards seven new subs
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
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2015
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Molecular Catalysis - B Enzymatic
ISSN
1381-1177
e-ISSN
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Volume of the periodical
122
Issue of the periodical within the volume
December
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
8
Pages from-to
240-247
UT code for WoS article
000366078800030
EID of the result in the Scopus database
2-s2.0-84944313586