Difference between revisions of "YIL160C"

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{|{{Prettytable}} align = 'right' width = '200px'
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YIL160C YIL160C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001422 YIL160C]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''POT1 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''POT1 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|nowrap| Chr IX:41444..40191
 
|nowrap| Chr IX:41444..40191
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000001422
 
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'''Description of {{PAGENAME}}:''' 3-ketoacyl-CoA thiolase with broad chain length specificity, cleaves 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA during beta-oxidation of fatty acids<ref name='S000058254'>Mathieu M, et al. (1997) The 1.8 A crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: implications for substrate binding and reaction mechanism. J Mol Biol 273(3):714-28
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'''Description of YIL160C:''' 3-ketoacyl-CoA thiolase with broad chain length specificity, cleaves 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA during beta-oxidation of fatty acids<ref name='S000058254'>Mathieu M, et al. (1997) The 1.8 A crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: implications for substrate binding and reaction mechanism. J Mol Biol 273(3):714-28
 
  {{SGDpaper|S000058254}} PMID 9402066</ref>
 
  {{SGDpaper|S000058254}} PMID 9402066</ref>
 
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J Biol Chem 278(5):3265-74</ref>
 
J Biol Chem 278(5):3265-74</ref>
 
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Latest revision as of 07:45, 23 January 2012

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Systematic name YIL160C
Gene name POT1
Aliases FOX3, POX3
Feature type ORF, Verified
Coordinates Chr IX:41444..40191
Primary SGDID S000001422


Description of YIL160C: 3-ketoacyl-CoA thiolase with broad chain length specificity, cleaves 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA during beta-oxidation of fatty acids[1]




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Community Commentary

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DNA and RNA Details

Other DNA and RNA Details

Other Topic: expression

Specifically higher expression in carbon limited chemostat cultures versus carbon excess. [2] [3]





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References

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  1. Mathieu M, et al. (1997) The 1.8 A crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: implications for substrate binding and reaction mechanism. J Mol Biol 273(3):714-28 SGD PMID 9402066
  2. 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. J Biol Chem 278(5):3265-74 SGD PMID 12414795
  3. submitted by Viktor Boer on 2003-07-25

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