Difference between revisions of "YGL040C"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003008 YGL040C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003008 YGL040C]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''HEM2 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''HEM2 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr VII:420561..419533
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|nowrap| Chr VII:420555..419527
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000003008
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000003008
 
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'''Description of YGL040C:''' Aminolevulinate dehydratase, a homo-octameric enzyme, catalyzes the conversion of 5-aminolevulinate to porphobilinogen, the second step in heme biosynthesis; enzymatic activity is zinc-dependent; localizes to the cytoplasm and nucleus<ref name='S000042491'>Myers AM, et al. (1987) Characterization of the yeast HEM2 gene and transcriptional regulation of COX5 and COR1 by heme. J Biol Chem 262(35):16822-9 {{SGDpaper|S000042491}} PMID 2445751</ref><ref name='S000046021'>Gollub EG, et al. (1977) Yeast mutants deficient in heme biosynthesis and a heme mutant additionally blocked in cyclization of 2,3-oxidosqualene. J Biol Chem 252(9):2846-54 {{SGDpaper|S000046021}} PMID 323256</ref><ref name='S000048328'>Borralho LM, et al. (1990) Purification of delta-aminolevulinate dehydratase from genetically engineered yeast. Yeast 6(4):319-30 {{SGDpaper|S000048328}} PMID 2204246</ref><ref name='S000074185'>Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91
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'''Description of YGL040C:''' Aminolevulinate dehydratase, a homo-octameric enzyme, catalyzes the conversion of 5-aminolevulinate to porphobilinogen, the second step in heme biosynthesis; enzymatic activity is zinc-dependent; localizes to the cytoplasm and nucleus<ref name='S000048328'>Borralho LM, et al. (1990) Purification of delta-aminolevulinate dehydratase from genetically engineered yeast. Yeast 6(4):319-30 {{SGDpaper|S000048328}} PMID 2204246</ref><ref name='S000046021'>Gollub EG, et al. (1977) Yeast mutants deficient in heme biosynthesis and a heme mutant additionally blocked in cyclization of 2,3-oxidosqualene. J Biol Chem 252(9):2846-54 {{SGDpaper|S000046021}} PMID 323256</ref><ref name='S000074185'>Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91 {{SGDpaper|S000074185}} PMID 14562095</ref><ref name='S000042491'>Myers AM, et al. (1987) Characterization of the yeast HEM2 gene and transcriptional regulation of COX5 and COR1 by heme. J Biol Chem 262(35):16822-9
  {{SGDpaper|S000074185}} PMID 14562095</ref>
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  {{SGDpaper|S000042491}} PMID 2445751</ref>
 
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Latest revision as of 07:45, 23 January 2012

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Systematic name YGL040C
Gene name HEM2
Aliases OLE4, SLU1
Feature type ORF, Verified
Coordinates Chr VII:420555..419527
Primary SGDID S000003008


Description of YGL040C: Aminolevulinate dehydratase, a homo-octameric enzyme, catalyzes the conversion of 5-aminolevulinate to porphobilinogen, the second step in heme biosynthesis; enzymatic activity is zinc-dependent; localizes to the cytoplasm and nucleus[1][2][3][4]




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References

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  1. Borralho LM, et al. (1990) Purification of delta-aminolevulinate dehydratase from genetically engineered yeast. Yeast 6(4):319-30 SGD PMID 2204246
  2. Gollub EG, et al. (1977) Yeast mutants deficient in heme biosynthesis and a heme mutant additionally blocked in cyclization of 2,3-oxidosqualene. J Biol Chem 252(9):2846-54 SGD PMID 323256
  3. Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91 SGD PMID 14562095
  4. Myers AM, et al. (1987) Characterization of the yeast HEM2 gene and transcriptional regulation of COX5 and COR1 by heme. J Biol Chem 262(35):16822-9 SGD PMID 2445751

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