Difference between revisions of "YGL148W"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YGL148W YGL148W]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003116 YGL148W]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''ARO2 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''ARO2 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr VII:226404..227534
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|nowrap| Chr VII:226399..227529
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000003116
 
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'''Description of {{PAGENAME}}:''' Bifunctional chorismate synthase and flavin reductase, catalyzes the conversion of 5-enolpyruvylshikimate 3-phosphate (EPSP) to form chorismate, which is a precursor to aromatic amino acids<ref name='S000070200'>Jones EW and Fink GR (1982) Regulation of amino acid and nucleotide biosynthesis in yeast. Pp.181-299 in The Molecular Biology of the Yeast Saccharomyces: Metabolism and Gene Expression, edited by Strathern JN, Jones EW and Broach JR. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press {{SGDpaper|S000070200}} PMID </ref><ref name='S000061725'>Henstrand JM, et al. (1996) Saccharomyces cerevisiae chorismate synthase has a flavin reductase activity. Mol Microbiol 22(5):859-66 {{SGDpaper|S000061725}} PMID 8971708</ref><ref name='S000054008'>Jones DG, et al. (1991) Molecular cloning, characterization and analysis of the regulation of the ARO2 gene, encoding chorismate synthase, of Saccharomyces cerevisiae. Mol Microbiol 5(9):2143-52
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'''Description of YGL148W:''' Bifunctional chorismate synthase and flavin reductase, catalyzes the conversion of 5-enolpyruvylshikimate 3-phosphate (EPSP) to form chorismate, which is a precursor to aromatic amino acids<ref name='S000061725'>Henstrand JM, et al. (1996) Saccharomyces cerevisiae chorismate synthase has a flavin reductase activity. Mol Microbiol 22(5):859-66 {{SGDpaper|S000061725}} PMID 8971708</ref><ref name='S000054008'>Jones DG, et al. (1991) Molecular cloning, characterization and analysis of the regulation of the ARO2 gene, encoding chorismate synthase, of Saccharomyces cerevisiae. Mol Microbiol 5(9):2143-52 {{SGDpaper|S000054008}} PMID 1837329</ref><ref name='S000070200'>Jones EW and Fink GR (1982) Regulation of amino acid and nucleotide biosynthesis in yeast. Pp.181-299 in The Molecular Biology of the Yeast Saccharomyces: Metabolism and Gene Expression, edited by Strathern JN, Jones EW and Broach JR. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
  {{SGDpaper|S000054008}} PMID 1837329</ref>
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  {{SGDpaper|S000070200}} PMID </ref>
 
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==Community Commentary==
 
==Community Commentary==
 
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Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
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<ref>Boer VM, et al. (2003) The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur.
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J Biol Chem 278(5):3265-74</ref>
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==References==
 
==References==
 
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Latest revision as of 07:45, 23 January 2012

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Systematic name YGL148W
Gene name ARO2
Aliases
Feature type ORF, Verified
Coordinates Chr VII:226399..227529
Primary SGDID S000003116


Description of YGL148W: Bifunctional chorismate synthase and flavin reductase, catalyzes the conversion of 5-enolpyruvylshikimate 3-phosphate (EPSP) to form chorismate, which is a precursor to aromatic amino acids[1][2][3]




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Community Commentary

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References

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  1. Henstrand JM, et al. (1996) Saccharomyces cerevisiae chorismate synthase has a flavin reductase activity. Mol Microbiol 22(5):859-66 SGD PMID 8971708
  2. Jones DG, et al. (1991) Molecular cloning, characterization and analysis of the regulation of the ARO2 gene, encoding chorismate synthase, of Saccharomyces cerevisiae. Mol Microbiol 5(9):2143-52 SGD PMID 1837329
  3. Jones EW and Fink GR (1982) Regulation of amino acid and nucleotide biosynthesis in yeast. Pp.181-299 in The Molecular Biology of the Yeast Saccharomyces: Metabolism and Gene Expression, edited by Strathern JN, Jones EW and Broach JR. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press SGD PMID

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