Overproduction and characterization of the first enzyme of a new aldoxime dehydratase family in Bradyrhizobium sp

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F18%3A00491995" target="_blank" >RIV/61388971:_____/18:00491995 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11310/18:10378082

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.ijbiomac.2018.04.103" target="_blank" >http://dx.doi.org/10.1016/j.ijbiomac.2018.04.103</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.ijbiomac.2018.04.103" target="_blank" >10.1016/j.ijbiomac.2018.04.103</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Overproduction and characterization of the first enzyme of a new aldoxime dehydratase family in Bradyrhizobium sp

Popis výsledku v původním jazyce

Almost 100 genes within the genus Bradyrhizobium are known to potentially encode aldoxime dehydratases (Oxds), but none of the corresponding proteins have been characterized yet. Aldoximes are natural substances involved in plant defense and auxin synthesis, and Oxds are components of enzymatic cascades enabling bacteria to transform, utilize and detoxify them. The aim of this work was to characterize a representative of the highly conserved Oxds in Bradyrhizobium spp. which include both plant symbionts and members of the soil communities. The selected oxd gene from Bradyrhizobium sp. LTSPM299 was expressed in Escherichia coli, and the corresponding gene product (OxdBr1, GenBank: WP_044589203) was obtained as an N-His(6)-tagged protein (monomer, 40.7 kDa) with 30-47% identity to Oxds characterized previously. OxdBrl was most stable at pH ca. 7.0-8.0 and at up to 30 degrees C. As substrates, the enzyme acted on (aryl)aliphatic aldoximes such as E/Z-phenylacetaldoxime, E/Z-2-phenylpropionaldoxime, E/Z-3-phenylpropionaldoxime, E/Z-indole-3-acetaldoxime, E/Z-propionaldoxime, E/Z-butyraldoxime, E/Z-valeraldoxime and E/Z-isovaleraldoxime. Some of the reaction products of OxdBrl are substrates of nitrilases occurring in the same genus. Regions upstream of the oxd gene contained genes encoding a putative aliphatic nitrilase and its transcriptional activator, indicating the participation of OxdBrl in the metabolic route from aldoximes to carboxylic acids.

Název v anglickém jazyce

Overproduction and characterization of the first enzyme of a new aldoxime dehydratase family in Bradyrhizobium sp

Popis výsledku anglicky

Almost 100 genes within the genus Bradyrhizobium are known to potentially encode aldoxime dehydratases (Oxds), but none of the corresponding proteins have been characterized yet. Aldoximes are natural substances involved in plant defense and auxin synthesis, and Oxds are components of enzymatic cascades enabling bacteria to transform, utilize and detoxify them. The aim of this work was to characterize a representative of the highly conserved Oxds in Bradyrhizobium spp. which include both plant symbionts and members of the soil communities. The selected oxd gene from Bradyrhizobium sp. LTSPM299 was expressed in Escherichia coli, and the corresponding gene product (OxdBr1, GenBank: WP_044589203) was obtained as an N-His(6)-tagged protein (monomer, 40.7 kDa) with 30-47% identity to Oxds characterized previously. OxdBrl was most stable at pH ca. 7.0-8.0 and at up to 30 degrees C. As substrates, the enzyme acted on (aryl)aliphatic aldoximes such as E/Z-phenylacetaldoxime, E/Z-2-phenylpropionaldoxime, E/Z-3-phenylpropionaldoxime, E/Z-indole-3-acetaldoxime, E/Z-propionaldoxime, E/Z-butyraldoxime, E/Z-valeraldoxime and E/Z-isovaleraldoxime. Some of the reaction products of OxdBrl are substrates of nitrilases occurring in the same genus. Regions upstream of the oxd gene contained genes encoding a putative aliphatic nitrilase and its transcriptional activator, indicating the participation of OxdBrl in the metabolic route from aldoximes to carboxylic acids.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10606 - Microbiology

Projekt

<a href="/cs/project/LD15107" target="_blank" >LD15107: Nové aldoximdehydratasy: izolace, charakterizace a využití pro biokatalytické moduly</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2018

Kód důvěrnosti údajů

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

Název periodika

International Journal of Biological Macromolecules

ISSN

0141-8130

e-ISSN

—

Svazek periodika

115

Číslo periodika v rámci svazku

AUG 2018

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

8

Strana od-do

746-753

Kód UT WoS článku

000438662500083

EID výsledku v databázi Scopus

2-s2.0-85046136167