Resolution of alpha/beta-amino acids by enantioselective penicillin G acylase from Achromobacter sp.

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/61388971:_____/15:00455568 RIV/00216224:14310/15:00085553

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

Resolution of alpha/beta-amino acids by enantioselective penicillin G acylase from Achromobacter sp.

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

Resolution of alpha/beta-amino acids by enantioselective penicillin G acylase from Achromobacter sp.

Popis výsledku anglicky

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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

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

Rok uplatnění

2015

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Molecular Catalysis - B Enzymatic

ISSN

1381-1177

e-ISSN

—

Svazek periodika

122

Číslo periodika v rámci svazku

December

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

8

Strana od-do

240-247

Kód UT WoS článku

000366078800030

EID výsledku v databázi Scopus

2-s2.0-84944313586