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

This title appears in the Scientific Report : 2004

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...

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.

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.