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@ARTICLE{Guterl:4648,
      author       = {Guterl, K. and Andexer, J.N. and Sehl, T. and von
                      Langermann, J. and Frindi-Wosch, I. and Rosenkranz, T. and
                      Fitter, J. and Gruber, K. and Kragl, U. and Eggert, T. and
                      Pohl, M.},
      title        = {{U}neven {T}wins: {C}omparison of two enantiocomplementary
                      hydroxynitrile lyases with a/ß--hydrolase fold},
      journal      = {Journal of biotechnology},
      volume       = {141},
      issn         = {0168-1656},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {PreJuSER-4648},
      year         = {2009},
      note         = {The authors thank Julich Chiral Solutions/Codexis for
                      providing MeHNL-DNA and MeHNL-Cys81Ala expressing E. coli
                      cells, Astrid Wirtz for HPLC measurements and Sabine
                      Kruschinski for technical assistance. This work was
                      partially supported by the BMBF in frame of project
                      "Biokatalytische Hydrocyanierung $\&$ Hydroformylierung
                      (BioHydroForm) FKZ 0313402C" and by the Deutsche
                      Forschungsgemeinschaft in frame of the research training
                      group "BioNoCo" GK 1166.},
      abstract     = {Hydroxynitrile lyases (HNLs) are applied in technical
                      processes for the synthesis of chiral cyanohydrins. Here we
                      describe the thorough characterization of the recently
                      discovered R-hydroxynitrile lyase from Arabidopsis thaliana
                      and its S-selective counterpart from Manihot esculenta
                      (MeHNL) concerning their properties relevant for technical
                      applications. The results are compared to available data of
                      the structurally related S-HNL from Hevea brasiliensis
                      (HbHNL), which is frequently applied in technical processes.
                      Whereas substrate ranges are highly similar for all three
                      enzymes, the stability of MeHNL with respect to higher
                      temperature and low pH-values is superior to the other HNLs
                      with alpha/beta-hydrolase fold. This enhanced stability is
                      supposed to be due to the ability of MeHNL to form tetramers
                      in solution, while HbHNL and AtHNL are dimers. The different
                      inactivation pathways, deduced by means of circular
                      dichroism, tryptophan fluorescence and static light
                      scattering further support these results. Our data suggest
                      different possibilities to stabilize MeHNL and AtHNL for
                      technical applications: whereas the application of crude
                      cell extracts is appropriate for MeHNL, AtHNL is stabilized
                      by addition of polyols. In addition, the molecular reason
                      for the inhibition of MeHNL and HbHNL by acetate could be
                      elucidated, whereas no such inhibition was observed with
                      AtHNL.},
      keywords     = {Acetonitriles: metabolism / Aldehyde-Lyases: chemistry /
                      Aldehyde-Lyases: genetics / Aldehyde-Lyases: metabolism /
                      Amino Acid Sequence / Arabidopsis: enzymology / Arabidopsis:
                      genetics / Enzyme Stability / Escherichia coli: genetics /
                      Hevea: enzymology / Hevea: genetics / Hydrogen-Ion
                      Concentration / Hydrolases: genetics / Manihot: enzymology /
                      Manihot: genetics / Molecular Sequence Data / Plant
                      Proteins: genetics / Plant Proteins: metabolism /
                      Recombinant Proteins: genetics / Recombinant Proteins:
                      metabolism / Stereoisomerism / Substrate Specificity /
                      Temperature / Time Factors / Acetonitriles (NLM Chemicals) /
                      Plant Proteins (NLM Chemicals) / Recombinant Proteins (NLM
                      Chemicals) / mandelonitrile (NLM Chemicals) / Hydrolases
                      (NLM Chemicals) / Aldehyde-Lyases (NLM Chemicals) / J
                      (WoSType)},
      cin          = {ISB-2},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ISB-2-20090406},
      pnm          = {Programm Biosoft},
      pid          = {G:(DE-Juel1)FUEK443},
      shelfmark    = {Biotechnology $\&$ Applied Microbiology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19433222},
      UT           = {WOS:000266672600012},
      doi          = {10.1016/j.jbiotec.2009.03.010},
      url          = {https://juser.fz-juelich.de/record/4648},
}