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   0 => Snowflake\Publications\Domain\Model\Publicationprototypepersistent entity (uid=22027, pid=124)
      originalId => protected22027 (integer)
      authors => protected'Heeb, N. V.; Hubeli, J.; Fleischmann, T.; Lienemann,&nbs
         p;P.; Nayyar, N.; Lal, R.; Kohler, H. P. E.' (144 chars)
      title => protected'Transformation of ε-HBCD with the <em>Sphingobium Indicum</em> enzymes LinA
         1, LinA2 and LinATM, a triple mutant of LinA2' (121 chars)
      journal => protected'Chemosphere' (11 chars)
      year => protected2021 (integer)
      volume => protected267 (integer)
      issue => protected'' (0 chars)
      startpage => protected'129217 (12 pp.)' (15 chars)
      otherpage => protected'' (0 chars)
      categories => protected'' (0 chars)
      description => protected'Hexabromocyclododecanes (HBCDs) were used as flame-retardants until their ba
         n in 2013. Among the 16 stereoisomers known, ε-HBCD has the highest symmetr
         y. This makes ε-HBCD an interesting substrate to study the selectivity of b
         iotransformations. We expressed three LinA dehydrohalogenase enzymes in <em>
         E. coli</em> bacteria, two wild-type, originating from <em>Sphingobium indic
         um</em> B90A bacteria and LinATM, a triple mutant of LinA2, with mutations o
         f L96C, F113Y and T133 M. These enzymes are involved in the hexachlorocycloh
         exane (HCH) metabolism, specifically of the insecticide γ-HCH (Lindane). We
          studied the reactivity of those eight HBCD stereoisomers found in technical
          HBCD. Furthermore, we compared kinetics and selectivity of these LinA varia
         nts with respect to ε-HBCD. LC-MS data indicate that all enzymes converted 
         ε-HBCD to pentabromocyclododecenes (PBCDens). Transformations followed Mich
         aelis-Menten kinetics. Rate constants k<sub>cat</sub> and enzyme specificiti
         es k<sub>cat</sub>/K<sub>M</sub> indicate that ε-HBCD conversion was fastes
         t and most specific with LinA2. Only one PBCDen stereoisomer was formed by L
         inA2, while LinA1 and LinATM produced mixtures of two PBCDE enantiomers at t
         
         
          assume that 1E,5S,6R,9S,10R-PBCDen is the ε-HBCD transformation product fr
         om LinA2. Implementing three amino acids of the LinA1 substrate-binding site
          into LinA2 resulted in a triple mutant with similar kinetics and product sp
         ecificity like LinA1. Thus, point-directed mutagenesis is an interesting too
         l to modify the substrate- and product-specificity of LinA enzymes and enlar
         ge their scope to metabolize other halogenated persistent organic pollutants
          regulated under the Stockholm Convention.' (1866 chars)
      serialnumber => protected'0045-6535' (9 chars)
      doi => protected'10.1016/j.chemosphere.2020.129217' (33 chars)
      uid => protected22027 (integer)
      _localizedUid => protected22027 (integer)modified
      _languageUid => protectedNULL
      _versionedUid => protected22027 (integer)modified
      pid => protected124 (integer)