FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2019916357> ?p ?o ?g. }

• W2019916357 endingPage "e93809" @default.
• W2019916357 startingPage "e93809" @default.
• W2019916357 abstract "Ectoine and hydroxyectoine are well-recognized members of the compatible solutes and are widely employed by microorganisms as osmostress protectants. The EctABC enzymes catalyze the synthesis of ectoine from the precursor L-aspartate-β-semialdehyde. A subgroup of the ectoine producers can convert ectoine into 5-hydroxyectoine through a region-selective and stereospecific hydroxylation reaction. This compatible solute possesses stress-protective and function-preserving properties different from those of ectoine. Hydroxylation of ectoine is carried out by the EctD protein, a member of the non-heme-containing iron (II) and 2-oxoglutarate-dependent dioxygenase superfamily. We used the signature enzymes for ectoine (EctC) and hydroxyectoine (EctD) synthesis in database searches to assess the taxonomic distribution of potential ectoine and hydroxyectoine producers. Among 6428 microbial genomes inspected, 440 species are predicted to produce ectoine and of these, 272 are predicted to synthesize hydroxyectoine as well. Ectoine and hydroxyectoine genes are found almost exclusively in Bacteria. The genome context of the ect genes was explored to identify proteins that are functionally associated with the synthesis of ectoines; the specialized aspartokinase Ask_Ect and the regulatory protein EctR. This comprehensive in silico analysis was coupled with the biochemical characterization of ectoine hydroxylases from microorganisms that can colonize habitats with extremes in salinity (Halomonas elongata), pH (Alkalilimnicola ehrlichii, Acidiphilium cryptum), or temperature (Sphingopyxis alaskensis, Paenibacillus lautus) or that produce hydroxyectoine very efficiently over ectoine (Pseudomonas stutzeri). These six ectoine hydroxylases all possess similar kinetic parameters for their substrates but exhibit different temperature stabilities and differ in their tolerance to salts. We also report the crystal structure of the Virgibacillus salexigens EctD protein in its apo-form, thereby revealing that the iron-free structure exists already in a pre-set configuration to incorporate the iron catalyst. Collectively, our work defines the taxonomic distribution and salient biochemical properties of the ectoine hydroxylase protein family and contributes to the understanding of its structure." @default.
• W2019916357 created "2016-06-24" @default.
• W2019916357 creator A5035710665 @default.
• W2019916357 creator A5046618148 @default.
• W2019916357 creator A5059413943 @default.
• W2019916357 creator A5064587433 @default.
• W2019916357 creator A5072628229 @default.
• W2019916357 creator A5077256764 @default.
• W2019916357 date "2014-04-08" @default.
• W2019916357 modified "2023-10-15" @default.
• W2019916357 title "Biochemical Properties of Ectoine Hydroxylases from Extremophiles and Their Wider Taxonomic Distribution among Microorganisms" @default.
• W2019916357 cites W1518290678 @default.
• W2019916357 cites W1580982499 @default.
• W2019916357 cites W1642602682 @default.
• W2019916357 cites W1903569580 @default.
• W2019916357 cites W1967039644 @default.
• W2019916357 cites W1969966985 @default.
• W2019916357 cites W1977514314 @default.
• W2019916357 cites W1982682366 @default.
• W2019916357 cites W1983548091 @default.
• W2019916357 cites W1983812869 @default.
• W2019916357 cites W1985076103 @default.
• W2019916357 cites W1986191025 @default.
• W2019916357 cites W1987675286 @default.
• W2019916357 cites W1996539906 @default.
• W2019916357 cites W2000840258 @default.
• W2019916357 cites W2000940940 @default.
• W2019916357 cites W2013193018 @default.
• W2019916357 cites W2016405093 @default.
• W2019916357 cites W2019931636 @default.
• W2019916357 cites W2020350008 @default.
• W2019916357 cites W2021758123 @default.
• W2019916357 cites W2027574280 @default.
• W2019916357 cites W2030709910 @default.
• W2019916357 cites W2031228090 @default.
• W2019916357 cites W2034638795 @default.
• W2019916357 cites W2037989529 @default.
• W2019916357 cites W2038840577 @default.
• W2019916357 cites W2039531605 @default.
• W2019916357 cites W2042915927 @default.
• W2019916357 cites W2042998656 @default.
• W2019916357 cites W2051854969 @default.
• W2019916357 cites W2052503730 @default.
• W2019916357 cites W2055043387 @default.
• W2019916357 cites W2058359737 @default.
• W2019916357 cites W2058488162 @default.
• W2019916357 cites W2073290767 @default.
• W2019916357 cites W2073481152 @default.
• W2019916357 cites W2073965776 @default.
• W2019916357 cites W2074241253 @default.
• W2019916357 cites W2082861469 @default.
• W2019916357 cites W2087211827 @default.
• W2019916357 cites W2089336118 @default.
• W2019916357 cites W2092870643 @default.
• W2019916357 cites W2095776200 @default.
• W2019916357 cites W2096215014 @default.
• W2019916357 cites W2106069035 @default.
• W2019916357 cites W2111151586 @default.
• W2019916357 cites W2112622077 @default.
• W2019916357 cites W2113513236 @default.
• W2019916357 cites W2116951543 @default.
• W2019916357 cites W2119388149 @default.
• W2019916357 cites W2123609173 @default.
• W2019916357 cites W2124679625 @default.
• W2019916357 cites W2125970631 @default.
• W2019916357 cites W2128586767 @default.
• W2019916357 cites W2129320477 @default.
• W2019916357 cites W2130479394 @default.
• W2019916357 cites W2131105782 @default.
• W2019916357 cites W2132935842 @default.
• W2019916357 cites W2138273994 @default.
• W2019916357 cites W2139007168 @default.
• W2019916357 cites W2140011169 @default.
• W2019916357 cites W2140292630 @default.
• W2019916357 cites W2140994581 @default.
• W2019916357 cites W2143011426 @default.
• W2019916357 cites W2144081223 @default.
• W2019916357 cites W2151107150 @default.
• W2019916357 cites W2151119760 @default.
• W2019916357 cites W2152007302 @default.
• W2019916357 cites W2155786911 @default.
• W2019916357 cites W2157795346 @default.
• W2019916357 cites W2162651138 @default.
• W2019916357 cites W2163029786 @default.
• W2019916357 cites W2163341755 @default.
• W2019916357 cites W2167489009 @default.
• W2019916357 cites W2168525678 @default.
• W2019916357 cites W2171433605 @default.
• W2019916357 cites W2172185686 @default.
• W2019916357 cites W2409105530 @default.
• W2019916357 cites W4253444818 @default.
• W2019916357 doi "https://doi.org/10.1371/journal.pone.0093809" @default.
• W2019916357 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3979721" @default.
• W2019916357 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24714029" @default.
• W2019916357 hasPublicationYear "2014" @default.
• W2019916357 type Work @default.
• W2019916357 sameAs 2019916357 @default.
• W2019916357 citedByCount "63" @default.

• next