Zobrazeno 1 - 10
of 123
pro vyhledávání: '"Maleylacetate reductase"'
Autor:
Boitumelo Setlhare, Mduduzi P. Mokoena, Ademola O. Olaniran, Ajit Kumar, Oladipupo A. Aregbesola
Publikováno v:
Applied Biochemistry and Microbiology. 57:656-665
In this study, two newly isolated 2,4-dichlorophenol(2,4-DCP)-degrading strains, Pseudomonas sp. KZNSA (PKZNSA) and Klebsiella pneumoniae KZNSA (KpKZNSA), were enriched from an activated sludge sample with a known history of contamination with chlori
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::61e9ddbe7316a5cd6e2cf88d3e471796
https://doi.org/10.1134/s0003683821050148
https://doi.org/10.1134/s0003683821050148
Autor:
Shasank Sekhar Swain
Publikováno v:
International Journal Bioautomation, Vol 17, Iss 4, Pp 217-226 (2013)
With the advent of biological research in the field of environmental science, several microbes were found to act as the most important biodegradable molecules. Maleylacetate reductase being a member of oxidoreductase is mostly found in Pseudomonas sp
Externí odkaz:
https://doaj.org/article/cbefabe6ebfe4497afec2ff7b725f563
Akademický článek
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Akademický článek
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Autor:
Yunhee Lee, Baolei Jia, Kyung Hyun Kim, Che Ok Jeon, Ju Hye Baek, Hyun Mi Jin, Sang Eun Jeong
Publikováno v:
SSRN Electronic Journal.
A new bacterium, Rhodococcus sp. S2-17, which could completely degrade the xenobiotic compound benzophenone-3 (BP-3), was isolated from contaminated sediment through an enrichment procedure, and its BP-3 catabolic pathway and genes were identified th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::61745a27ae497273124e83b4179b6897
https://doi.org/10.2139/ssrn.3952431
https://doi.org/10.2139/ssrn.3952431
Autor:
Sabrina di Monaco, Heather T. Scott, Gabriela F. Persinoti, James J. Williamson, Edward Spence, Louison Dumond, Leonides A. Calvo-Bado, Fabio M. Squina, Timothy D. H. Bugg
Publikováno v:
Appl Environ Microbiol
Deletion of the pcaHG genes, encoding protocatechuate 3,4-dioxygenase in Rhodococcus jostii RHA1, gives a gene deletion strain still able to grow on protocatechuic acid as the sole carbon source, indicating a second degradation pathway for protocatec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a87c0164f55a3786f848c0f33615f56
https://europepmc.org/articles/PMC7499046/
https://europepmc.org/articles/PMC7499046/
Publikováno v:
FEBS J
Promiscuity is the coincidental ability of an enzyme to catalyze its native reaction and additional reactions that are not biological functions in the same active site. Promiscuity plays a central role in enzyme evolution and is thus a useful propert
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e7929d4bc337881d12ea2a6a90fbc359
https://europepmc.org/articles/PMC7245361/
https://europepmc.org/articles/PMC7245361/
Autor:
Haseeb A. Khan, Lifeng Chen, Meena Kishore Sakharkar, Jian Yang, Abdullah S. Alhomida, Ed S. Krol
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
Scientific Reports
Scientific Reports
Maleylacetate reductase (PcpE), the last enzyme in the pentachlorophenol biodegradation pathway in Sphingobium chlorophenolicum L-1, catalyzes two consecutive reductive reactions, reductive dehalogenation of 2-chloromaleylacetate (2-CMA) to maleylace
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0065948fb68a63d1dcfcd770f0c4fc21
http://link.springer.com/article/10.1038/s41598-017-18475-8
http://link.springer.com/article/10.1038/s41598-017-18475-8
Autor:
Yuko Okamoto, Masahiro Yoshida, Tomomi Fujii, Ai Sato, Yasuo Hata, Takae Yamauchi, Shiro Kato, Tadao Oikawa
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 84:1029-1042
Maleylacetate reductase plays a crucial role in catabolism of resorcinol by catalyzing the NAD(P)H-dependent reduction of maleylacetate, at a carbon-carbon double bond, to 3-oxoadipate. The crystal structure of maleylacetate reductase from Rhizobium
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5a4f13525d2acb31e2ed33f2b55c49c3
https://doi.org/10.1002/prot.25046
https://doi.org/10.1002/prot.25046
Autor:
Xiaoxia Zang, Yang Mu, Qing Chen, Yanzheng Gao, Wei-Bin Jia, Kai Chen, Zhuang Ke, Jiandong Jiang, Shanshan Jian
Publikováno v:
Applied and Environmental Microbiology. 84
The compound 3,5-dibromo-4-hydroxybenzoate (DBHB) is both anthropogenically released into and naturally produced in the environment, and its environmental fate is of great concern. Aerobic and anaerobic reductive dehalogenations are the only two repo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e71991161bbc18db2131b20f8e855fca
https://doi.org/10.1128/aem.02467-17
https://doi.org/10.1128/aem.02467-17