Difference between revisions of "YDR232W"
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{|{{Prettytable}} align = 'right' width = '200px' | {|{{Prettytable}} align = 'right' width = '200px' | ||
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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=S000002640 YDR232W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''HEM1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''HEM1 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr IV: | + | |nowrap| Chr IV:927452..929098 |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000002640 | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000002640 | ||
Latest revision as of 07:45, 23 January 2012
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| Systematic name | YDR232W |
| Gene name | HEM1 |
| Aliases | CYD1, OLE3 |
| Feature type | ORF, Verified |
| Coordinates | Chr IV:927452..929098 |
| Primary SGDID | S000002640 |
Description of YDR232W: 5-aminolevulinate synthase, catalyzes the first step in the heme biosynthetic pathway; an N-terminal signal sequence is required for localization to the mitochondrial matrix; expression is regulated by Hap2p-Hap3p[1][2][3][4][5][6]
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References
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- ↑ 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
- ↑ Haldi M and Guarente L (1989) N-terminal deletions of a mitochondrial signal sequence in yeast. Targeting information of delta-aminolevulinate synthase is encoded in non-overlapping regions. J Biol Chem 264(29):17107-12 SGD PMID 2507539
- ↑ Keng T and Guarente L (1987) Constitutive expression of the yeast HEM1 gene is actually a composite of activation and repression. Proc Natl Acad Sci U S A 84(24):9113-7 SGD PMID 3321068
- ↑ Keng T, et al. (1986) The nine amino-terminal residues of delta-aminolevulinate synthase direct beta-galactosidase into the mitochondrial matrix. Mol Cell Biol 6(2):355-64 SGD PMID 3023841
- ↑ Urban-Grimal D and Labbe-Bois R (1981) Genetic and biochemical characterization of mutants of Saccharomyces cerevisiae blocked in six different steps of heme biosynthesis. Mol Gen Genet 183(1):85-92 SGD PMID 7035824
- ↑ Urban-Grimal D, et al. (1986) The nucleotide sequence of the HEM1 gene and evidence for a precursor form of the mitochondrial 5-aminolevulinate synthase in Saccharomyces cerevisiae. Eur J Biochem 156(3):511-9 SGD PMID 3516694
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