Probing enzyme promiscuity of SGNH hydrolases.

@article{Aler2010ProbingEP,
  title={Probing enzyme promiscuity of SGNH hydrolases.},
  author={Ivana Le{\vs}{\vc}i{\'c} A{\vs}ler and Nives Ivi{\'c} and Filip Kova{\vc}i{\'c} and Sabrina Schell and Janina Knorr and Ulrich Krauss and Susanne Wilhelm and Biserka Kojic-Prodic and K. -E. J{\"a}ger},
  journal={Chembiochem : a European journal of chemical biology},
  year={2010},
  volume={11 15},
  pages={
          2158-67
        }
}
Several hydrolases of the SGNH superfamily, including the lipase SrLip from Streptomyces rimosus (Q93MW7), the acyl-CoA thioesterase I TesA from Pseudomonas aeruginosa (Q9HZY8) and the two lipolytic enzymes EstA (from P. aeruginosa, O33407) and EstP (from Pseudomonas putida, Q88QS0), were examined for promiscuity. These enzymes were tested against four chemically different classes of a total of 34 substrates known to be hydrolysed by esterases, thioesterases, lipases, phospholipases, Tweenases… CONTINUE READING
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