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@ARTICLE{Schlsser:32554,
      author       = {Schlösser, T. and Gätgens, C. and Weber, U. and Stahmann,
                      K. P.},
      title        = {{A}lanine: glyoxylate aminotransferase of {S}accharomyces
                      cerevisiae - encoding gene {AGX}1 and metabolic
                      significance},
      journal      = {Yeast},
      volume       = {21},
      issn         = {0749-503X},
      address      = {New York, NY [u.a.]},
      publisher    = {Wiley},
      reportid     = {PreJuSER-32554},
      pages        = {63 - 73},
      year         = {2004},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Alanine : glyoxylate aminotransferase is one of three
                      different enzymes used for glycine synthesis in
                      Saccharomyces cerevisiae. The open reading frame YFL030w
                      (named AGX1 in the following), encoding this enzyme, was
                      identified by comparing enzyme specific activities in
                      knockout strains. While $100\%$ activity was detectable in
                      the parental strain, $2\%$ was found in a YFL030w::kanMX4
                      strain. The ORF found at that locus was suspected to encode
                      alanine : glyoxylate aminotransferase because its predicted
                      amino acid sequence showed $23\%$ identity to the human
                      homologue. Since the YFL030w::kanMX4 strain showed no
                      glycine auxtrophic phenotype, AGX1 was replaced by KanMX4 in
                      a Delta GLY1 Delta SHM1 Delta SHM2 background. These
                      background mutations, which cause inactivation of threonine
                      aldolase, mitochondrial and cytosolic serine
                      hydroxymethyltransferase, respectively, lead to a
                      conditional glycine auxotrophy. This means that growth is
                      not possible on glucose but on ethanol as the sole carbon
                      source. Additional disruption of AGX1 revealed a complete
                      glycine auxotrophy. Complementation was observed by
                      transformation with a plasmid-encoded AGX1.},
      keywords     = {Alanine: metabolism / Amino Acid Sequence / Animals / Base
                      Sequence / DNA, Fungal: chemistry / DNA, Fungal: genetics /
                      Glycine: biosynthesis / Glyoxylates: metabolism / Humans /
                      Models, Chemical / Molecular Sequence Data / Mutagenesis,
                      Insertional / Orotic Acid: analogs $\&$ derivatives / Orotic
                      Acid: metabolism / Saccharomyces cerevisiae: enzymology /
                      Saccharomyces cerevisiae: genetics / Selection, Genetic /
                      Sequence Alignment / Transaminases: genetics /
                      Transaminases: metabolism / DNA, Fungal (NLM Chemicals) /
                      Glyoxylates (NLM Chemicals) / glyoxylic acid (NLM Chemicals)
                      / Glycine (NLM Chemicals) / Alanine (NLM Chemicals) / Orotic
                      Acid (NLM Chemicals) / 5-fluoroorotic acid (NLM Chemicals) /
                      Transaminases (NLM Chemicals) / Alanine-glyoxylate
                      transaminase (NLM Chemicals) / J (WoSType)},
      cin          = {IBT-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB55},
      pnm          = {Biotechnologie},
      pid          = {G:(DE-Juel1)FUEK256},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Biotechnology $\&$
                      Applied Microbiology / Microbiology / Mycology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:14745783},
      UT           = {WOS:000188635600006},
      doi          = {10.1002/yea.1058},
      url          = {https://juser.fz-juelich.de/record/32554},
}