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@ARTICLE{Piotrowski:23567,
      author       = {Piotrowski, M. and Janowitz, T. and Kneifel, H.},
      title        = {{P}lant {C}-{N}-{H}ydrolases and the identification of a
                      plant {N}-{C}arbamoylputrescine amidohydrolase involved in
                      polyamine biosynthesis},
      journal      = {The journal of biological chemistry},
      volume       = {278},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {PreJuSER-23567},
      pages        = {1708 - 1712},
      year         = {2003},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {A nitrilase-like protein from Arabidopsis thaliana (NLP1)
                      was expressed in Escherichia coli as a His(6)-tagged protein
                      and purified to apparent homogeneity by Ni(2+)-chelate
                      affinity chromatography. The purified enzyme showed
                      N-carbamoylputrescine amidohydrolase activity, an enzyme
                      involved in the biosynthesis of polyamines in plants and
                      bacteria. N-carbamoylputrescine amidohydrolase activity was
                      confirmed by identification of two of the three occurring
                      products, namely putrescine and ammonia. In contrast, no
                      enzymatic activity could be detected when applying various
                      compounds including nitriles, amines, and amides as well as
                      other N-carbamoyl compounds, indicating the specificity of
                      the enzyme for N-carbamoylputrescine. Like the homologous
                      beta-alanine synthases, NLP1 showed positive cooperativity
                      toward its substrate. The native enzyme had a molecular mass
                      of 279 kDa as shown by blue-native polyacrylamide gel
                      electrophoresis, indicating a complex of eight monomers.
                      Expression of the NLP1 gene was found in all organs
                      investigated, but it was not induced upon osmotic stress,
                      which is known to induce biosynthesis of putrescine. This is
                      the first report of cloning and expression of a plant
                      N-carbamoylputrescine amidohydrolase and the first time that
                      N-carbamoylputrescine amidohydrolase activity of a
                      recombinant protein could be shown in vitro. NLP1 is one of
                      the two missing links in the arginine decarboxylase pathway
                      of putrescine biosynthesis in higher plants.},
      keywords     = {Arabidopsis: enzymology / Biogenic Polyamines: biosynthesis
                      / Blotting, Northern / Electrophoresis, Polyacrylamide Gel /
                      Mass Spectrometry / Phylogeny / Ureohydrolases: chemistry /
                      Ureohydrolases: genetics / Ureohydrolases: metabolism /
                      Biogenic Polyamines (NLM Chemicals) / N-carbamoylputrescine
                      hydrolase (NLM Chemicals) / Ureohydrolases (NLM Chemicals) /
                      J (WoSType)},
      cin          = {ICG-III},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB49},
      pnm          = {Chemie und Dynamik der Geo-Biosphäre},
      pid          = {G:(DE-Juel1)FUEK257},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:12435743},
      UT           = {WOS:000180462200046},
      doi          = {10.1074/jbc.M205699200},
      url          = {https://juser.fz-juelich.de/record/23567},
}