YGL040C - Revision history

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@@ Line 4: / Line 4: @@
 {|{{Prettytable}} align = 'right' width = '200px'
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003008 YGL040C]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003008 YGL040C]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''HEM2 ''

@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr VII:420561..419533
+|nowrap| Chr VII:420555..419527
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000003008

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''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
+'''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>
+  {{SGDpaper|S000042491}} PMID 2445751</ref>
 <br>
 <br>

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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''HEM2 ''
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases'''           ||''SLU1''
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases'''           ||''OLE4, SLU1''
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type'''           || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YGL040C:''' Delta-aminolevulinate dehydratase, a homo-octameric enzyme, catalyzes the conversion of delta-aminolevulinic acid to porphobilinogen, the second step in the heme biosynthetic pathway; localizes to both 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
+'''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
   {{SGDpaper|S000074185}} PMID 14562095</ref>
 <br>

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		+	Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
		+	<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.
		+	J Biol Chem 278(5):3265-74</ref>
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