Biotransformation of nitriles to hydroxamic acids via a nitrile hydratase?amidase cascade reaction

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F11%3A00360786" target="_blank" >RIV/61388971:_____/11:00360786 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.molcatb.2011.03.008" target="_blank" >http://dx.doi.org/10.1016/j.molcatb.2011.03.008</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.molcatb.2011.03.008" target="_blank" >10.1016/j.molcatb.2011.03.008</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Biotransformation of nitriles to hydroxamic acids via a nitrile hydratase?amidase cascade reaction

Popis výsledku v původním jazyce

The transformation of benzonitrile into benzohydroxamic acid was performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step was catalyzed by either a cell-free extract from Rhodococcus erythropolis A4 (nitrile hydratase) or cell-free extracts from recombinant Escherichia coli strains expressing nitrile hydratases from Raoultella terrigena 77.1 and Klebsiella oxytoca 38.1.2; the biocatalyst in the second stepwas a cellfree extract from R. erythropolis A4 (amidase). When using the cell-free extract from R. erythropolis A4 in the first step, the hydrolytic amidase activity was suppressed by ammonium ions, which, however, did not inhibit the acyl transfer reaction catalyzed by the same enzyme. Aromatic and aliphatic nitriles were examined as substrates of the recombinant nitrile hydratases by using a colorimetric assay of hydroxamic acids produced in a coupled acyl transfer reaction

Název v anglickém jazyce

Biotransformation of nitriles to hydroxamic acids via a nitrile hydratase?amidase cascade reaction

Popis výsledku anglicky

The transformation of benzonitrile into benzohydroxamic acid was performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step was catalyzed by either a cell-free extract from Rhodococcus erythropolis A4 (nitrile hydratase) or cell-free extracts from recombinant Escherichia coli strains expressing nitrile hydratases from Raoultella terrigena 77.1 and Klebsiella oxytoca 38.1.2; the biocatalyst in the second stepwas a cellfree extract from R. erythropolis A4 (amidase). When using the cell-free extract from R. erythropolis A4 in the first step, the hydrolytic amidase activity was suppressed by ammonium ions, which, however, did not inhibit the acyl transfer reaction catalyzed by the same enzyme. Aromatic and aliphatic nitriles were examined as substrates of the recombinant nitrile hydratases by using a colorimetric assay of hydroxamic acids produced in a coupled acyl transfer reaction

Druh

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

CEP obor

EE - Mikrobiologie, virologie

OECD FORD obor

—

Projekt

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

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2011

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

71

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

5

Strana od-do

51-55

Kód UT WoS článku

000291451000008

EID výsledku v databázi Scopus

—