Overproduction and characterization of the first enzyme of a new aldoxime dehydratase family in Bradyrhizobium sp
The result's identifiers
Result code in 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>
Alternative codes found
RIV/00216208:11310/18:10378082
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
Overproduction and characterization of the first enzyme of a new aldoxime dehydratase family in Bradyrhizobium sp
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10606 - Microbiology
Result continuities
Project
<a href="/en/project/LD15107" target="_blank" >LD15107: New aldoxime dehydratases: isolation, characterization and use in biocatalytic modules</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2018
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
International Journal of Biological Macromolecules
ISSN
0141-8130
e-ISSN
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Volume of the periodical
115
Issue of the periodical within the volume
AUG 2018
Country of publishing house
GB - UNITED KINGDOM
Number of pages
8
Pages from-to
746-753
UT code for WoS article
000438662500083
EID of the result in the Scopus database
2-s2.0-85046136167