Difference between revisions of "YGL040C"
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| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http:// | + | |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: | + | |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=' | + | '''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| | + | {{SGDpaper|S000042491}} PMID 2445751</ref> |
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Latest revision as of 06:45, 23 January 2012
Share your knowledge...Edit this entry! <protect>
| 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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- ↑ Borralho LM, et al. (1990) Purification of delta-aminolevulinate dehydratase from genetically engineered yeast. Yeast 6(4):319-30 SGD PMID 2204246
- ↑ 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
- ↑ Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91 SGD PMID 14562095
- ↑ 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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