FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W3183253657> ?p ?o ?g. }

• W3183253657 abstract "Arylamines constitute a large group of industrial chemicals detoxified by certain bacteria through conjugation reactions catalyzed by N-acetyltransferase (NAT) enzymes. NAT homologs, mostly from pathogenic bacteria, have been the subject of individual studies that do not lend themselves to direct comparisons. By implementing a practicable pipeline, we carried out a comparative investigation of 15 NAT homologs from 10 bacteria, mainly bacilli, streptomycetes, and one alphaproteobacterium. The new homologs were characterized for their sequence, phylogeny, predicted structural features, substrate specificity, thermal stability, and interaction with components of the enzymatic reaction. Bacillus NATs demonstrated the characteristics of xenobiotic metabolizing N-acetyltransferases, with the majority of homologs generating high activities. Nonpathogenic bacilli are thus proposed as suitable mediators of arylamine bioremediation. Of the Streptomyces homologs, the NAT2 isoenzyme of S. venezuelae efficiently transformed highly toxic arylamines, while the remaining homologs were inactive or generated low activities, suggesting that xenobiotic metabolism may not be their primary role. The functional divergence of Streptomyces NATs was consistent with their observed sequence, phylogenetic, and structural variability. These and previous findings support classification of microbial NATs into three groups. The first includes xenobiotic metabolizing enzymes with dual acetyl/propionyl coenzyme A (CoA) selectivity. Homologs of the second group are more rarely encountered, acting as malonyltransferases mediating specialized ecological interactions. Homologs of the third group effectively lack acyltransferase activity, and their study may represent an interesting research area. Comparative NAT enzyme screens from a broad microbial spectrum may guide rational selection of homologs likely to share similar biological functions, allowing their combined investigation and use in biotechnological applications. IMPORTANCE Arylamines are encountered as industrial chemicals or by-products of agrochemicals that may constitute highly toxic contaminants of soils and groundwaters. Although such chemicals may be recalcitrant to biotransformation, they can be enzymatically converted into less toxic forms by some bacteria. Therefore, exploitation of the arylamine detoxification capabilities of microorganisms is investigated as an effective approach for bioremediation. Among microbial biotransformations of arylamines, enzymatic conjugation reactions have been reported, including NAT-mediated N-acetylation. Comparative investigations of NAT enzymes across a range of microorganisms can be laborious and expensive, so here we present a streamlined methodology for implementing such work. We compared 15 NAT homologs from nonpathogenic, free-living bacteria of potential biotechnological utility, mainly Terrabacteria, which are known for their rich secondary and xenobiotic metabolism. The analysis allowed insights into the evolutionary and functional divergence of bacterial NAT homologs, combined with assessment of their fundamental structural and enzymatic differences and similarities." @default.
• W3183253657 created "2021-08-02" @default.
• W3183253657 creator A5008091638 @default.
• W3183253657 creator A5009319585 @default.
• W3183253657 creator A5021230584 @default.
• W3183253657 creator A5028340844 @default.
• W3183253657 creator A5040187707 @default.
• W3183253657 creator A5060074985 @default.
• W3183253657 creator A5082701673 @default.
• W3183253657 creator A5084341946 @default.
• W3183253657 date "2021-09-10" @default.
• W3183253657 modified "2023-10-17" @default.
• W3183253657 title "Comparative Investigation of 15 Xenobiotic-Metabolizing <i>N</i> -Acetyltransferase (NAT) Homologs from Bacteria" @default.
• W3183253657 cites W1231658740 @default.
• W3183253657 cites W1491175805 @default.
• W3183253657 cites W1499743159 @default.
• W3183253657 cites W1924301698 @default.
• W3183253657 cites W1968791898 @default.
• W3183253657 cites W1978428288 @default.
• W3183253657 cites W1993923156 @default.
• W3183253657 cites W1996869967 @default.
• W3183253657 cites W1999646367 @default.
• W3183253657 cites W2000106654 @default.
• W3183253657 cites W2001183484 @default.
• W3183253657 cites W2003146628 @default.
• W3183253657 cites W2014156628 @default.
• W3183253657 cites W2036159390 @default.
• W3183253657 cites W2040470955 @default.
• W3183253657 cites W2041092576 @default.
• W3183253657 cites W2043512288 @default.
• W3183253657 cites W2047698915 @default.
• W3183253657 cites W2053419614 @default.
• W3183253657 cites W2054404209 @default.
• W3183253657 cites W2063360787 @default.
• W3183253657 cites W2065619930 @default.
• W3183253657 cites W2069009374 @default.
• W3183253657 cites W2074093254 @default.
• W3183253657 cites W2076532204 @default.
• W3183253657 cites W2083412871 @default.
• W3183253657 cites W2083598610 @default.
• W3183253657 cites W2085774588 @default.
• W3183253657 cites W2086266184 @default.
• W3183253657 cites W2086476198 @default.
• W3183253657 cites W2088111804 @default.
• W3183253657 cites W2088732615 @default.
• W3183253657 cites W2089258924 @default.
• W3183253657 cites W2093127234 @default.
• W3183253657 cites W2094499969 @default.
• W3183253657 cites W2100357455 @default.
• W3183253657 cites W2103808653 @default.
• W3183253657 cites W2110045183 @default.
• W3183253657 cites W2110827590 @default.
• W3183253657 cites W2111984972 @default.
• W3183253657 cites W2113202957 @default.
• W3183253657 cites W2118335777 @default.
• W3183253657 cites W2125121305 @default.
• W3183253657 cites W2128585170 @default.
• W3183253657 cites W2128739919 @default.
• W3183253657 cites W2130303232 @default.
• W3183253657 cites W2133660802 @default.
• W3183253657 cites W2133700798 @default.
• W3183253657 cites W2142280385 @default.
• W3183253657 cites W2149298729 @default.
• W3183253657 cites W2150253241 @default.
• W3183253657 cites W2150704873 @default.
• W3183253657 cites W2168974130 @default.
• W3183253657 cites W2554207773 @default.
• W3183253657 cites W2795937328 @default.
• W3183253657 cites W2796274201 @default.
• W3183253657 cites W2809663710 @default.
• W3183253657 cites W2927961455 @default.
• W3183253657 cites W2982352424 @default.
• W3183253657 cites W4248064487 @default.
• W3183253657 doi "https://doi.org/10.1128/aem.00819-21" @default.
• W3183253657 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8432529" @default.
• W3183253657 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/34288706" @default.
• W3183253657 hasPublicationYear "2021" @default.
• W3183253657 type Work @default.
• W3183253657 sameAs 3183253657 @default.
• W3183253657 citedByCount "4" @default.
• W3183253657 countsByYear W31832536572022 @default.
• W3183253657 countsByYear W31832536572023 @default.
• W3183253657 crossrefType "journal-article" @default.
• W3183253657 hasAuthorship W3183253657A5008091638 @default.
• W3183253657 hasAuthorship W3183253657A5009319585 @default.
• W3183253657 hasAuthorship W3183253657A5021230584 @default.
• W3183253657 hasAuthorship W3183253657A5028340844 @default.
• W3183253657 hasAuthorship W3183253657A5040187707 @default.
• W3183253657 hasAuthorship W3183253657A5060074985 @default.
• W3183253657 hasAuthorship W3183253657A5082701673 @default.
• W3183253657 hasAuthorship W3183253657A5084341946 @default.
• W3183253657 hasBestOaLocation W31832536572 @default.
• W3183253657 hasConcept C104317684 @default.
• W3183253657 hasConcept C115448650 @default.
• W3183253657 hasConcept C119157956 @default.
• W3183253657 hasConcept C135763542 @default.
• W3183253657 hasConcept C181199279 @default.
• W3183253657 hasConcept C182516595 @default.
• W3183253657 hasConcept C2778328694 @default.
• W3183253657 hasConcept C2779649592 @default.

• next