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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

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

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

  • 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