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@ARTICLE{Marienhagen:47527,
      author       = {Marienhagen, J. and Kennerknecht, N. and Sahm, H. and
                      Eggeling, L.},
      title        = {{F}unctional analysis of all aminotransferase proteins
                      inferred from the genome sequence of {C}orynebacterium
                      glutamicum},
      journal      = {Journal of bacteriology},
      volume       = {187},
      issn         = {0021-9193},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {PreJuSER-47527},
      pages        = {7639 - 7646},
      year         = {2005},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Twenty putative aminotransferase (AT) proteins of
                      Corynebacterium glutamicum, or rather pyridoxal-5'-phosphate
                      (PLP)-dependent enzymes, were isolated and assayed among
                      others with L-glutamate, L-aspartate, and L-alanine as amino
                      donors and a number of 2-oxo-acids as amino acceptors. One
                      outstanding AT identified is AlaT, which has a broad amino
                      donor specificity utilizing (in the order of preference)
                      L-glutamate > 2-aminobutyrate > L-aspartate with pyruvate as
                      acceptor. Another AT is AvtA, which utilizes L-alanine to
                      aminate 2-oxo-isovalerate, the L-valine precursor, and
                      2-oxo-butyrate. A second AT active with the L-valine
                      precursor and that of the other two branched-chain amino
                      acids, too, is IlvE, and both enzyme activities overlap
                      partially in vivo, as demonstrated by the analysis of
                      deletion mutants. Also identified was AroT, the aromatic AT,
                      and this and IlvE were shown to have comparable activities
                      with phenylpyruvate, thus demonstrating the relevance of
                      both ATs for L-phenylalanine synthesis. We also assessed the
                      activity of two PLP-containing cysteine desulfurases,
                      supplying a persulfide intermediate. One of them is SufS,
                      which assists in the sulfur transfer pathway for the Fe-S
                      cluster assembly. Together with the identification of
                      further ATs and the additional analysis of deletion mutants,
                      this results in an overview of the ATs within an organism
                      that may not have been achieved thus far.},
      keywords     = {Alanine: metabolism / Aspartic Acid: metabolism / Bacterial
                      Proteins: genetics / Bacterial Proteins: isolation $\&$
                      purification / Bacterial Proteins: metabolism / Butyric
                      Acids: metabolism / Carbon-Sulfur Lyases: metabolism /
                      Corynebacterium glutamicum: enzymology / Corynebacterium
                      glutamicum: genetics / Gene Deletion / Glutamic Acid:
                      metabolism / Keto Acids: metabolism / Phenylpyruvic Acids:
                      metabolism / Pyruvic Acid: metabolism / Substrate
                      Specificity / Transaminases: genetics / Transaminases:
                      isolation $\&$ purification / Transaminases: metabolism /
                      Bacterial Proteins (NLM Chemicals) / Butyric Acids (NLM
                      Chemicals) / Keto Acids (NLM Chemicals) / Phenylpyruvic
                      Acids (NLM Chemicals) / Pyruvic Acid (NLM Chemicals) /
                      alpha-keto-beta-methylvaleric acid (NLM Chemicals) /
                      phenylpyruvic acid (NLM Chemicals) / Alanine (NLM Chemicals)
                      / Aspartic Acid (NLM Chemicals) / Glutamic Acid (NLM
                      Chemicals) / alpha-ketobutyric acid (NLM Chemicals) /
                      alpha-ketoisovalerate (NLM Chemicals) / alpha-ketoisocaproic
                      acid (NLM Chemicals) / Transaminases (NLM Chemicals) /
                      Carbon-Sulfur Lyases (NLM Chemicals) / cysteine desulfurase
                      (NLM Chemicals) / J (WoSType)},
      cin          = {IBT-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB55},
      pnm          = {Biotechnologie},
      pid          = {G:(DE-Juel1)FUEK256},
      shelfmark    = {Microbiology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:16267288},
      pmc          = {pmc:PMC1280304},
      UT           = {WOS:000233400200011},
      doi          = {10.1128/JB.187.22.7639-7646.2005},
      url          = {https://juser.fz-juelich.de/record/47527},
}