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This title appears in the Scientific Report : 2004 

Alanine: glyoxylate aminotransferase of Saccharomyces cerevisiae - encoding gene AGX1 and metabolic significance

Alanine: glyoxylate aminotransferase of Saccharomyces cerevisiae - encoding gene AGX1 and metabolic significance

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% a...

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Personal Name(s): Schlösser, T.
Gätgens, C. / Weber, U. / Stahmann, K. P.
Contributing Institute: Biotechnologie 1; IBT-1
Published in: Yeast, 21 (2004) S. 63 - 73
Imprint: New York, NY [u.a.] Wiley 2004
Physical Description: 63 - 73
DOI: 10.1002/yea.1058
PubMed ID: 14745783
Document Type: Journal Article
Research Program: Biotechnologie
Series Title: Yeast 21
Subject (ZB):
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
Glyoxylates
glyoxylic acid
Glycine
Alanine
Orotic Acid
5-fluoroorotic acid
Transaminases
Alanine-glyoxylate transaminase
J
alanine : glyoxylate aminotransferase
glycine biosynthesis
amino acid metabolism
Saccharomyces cerevisiae
fungi
Publikationsportal JuSER
Please use the identifier: http://dx.doi.org/10.1002/yea.1058 in citations.

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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.

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