Difference between revisions of "YER175C"
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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=S000000977 YER175C] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''TMT1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''TMT1 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr V: | + | |nowrap| Chr V:540363..539464 |
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| + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000000977 | ||
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<br> | <br> | ||
| − | '''Description of | + | '''Description of YER175C:''' Trans-aconitate methyltransferase, cytosolic enzyme that catalyzes the methyl esterification of 3-isopropylmalate, an intermediate of the leucine biosynthetic pathway, and trans-aconitate, which inhibits the citric acid cycle<ref name='S000066185'>Cai H, et al. (2001) Identification of the gene and characterization of the activity of the trans-aconitate methyltransferase from Saccharomyces cerevisiae. Biochemistry 40(45):13699-709 {{SGDpaper|S000066185}} PMID 11695919</ref><ref name='S000076422'>Katz JE, et al. (2004) 3-Isopropylmalate is the major endogenous substrate of the Saccharomyces cerevisiae trans-aconitate methyltransferase. Biochemistry 43(20):5976-86 |
| − | {{SGDpaper| | + | {{SGDpaper|S000076422}} PMID 15147181</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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<protect> | <protect> | ||
Latest revision as of 06:45, 23 January 2012
Share your knowledge...Edit this entry! <protect>
| Systematic name | YER175C |
| Gene name | TMT1 |
| Aliases | TAM1 |
| Feature type | ORF, Verified |
| Coordinates | Chr V:540363..539464 |
| Primary SGDID | S000000977 |
Description of YER175C: Trans-aconitate methyltransferase, cytosolic enzyme that catalyzes the methyl esterification of 3-isopropylmalate, an intermediate of the leucine biosynthetic pathway, and trans-aconitate, which inhibits the citric acid cycle[1][2]
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References
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- ↑ Cai H, et al. (2001) Identification of the gene and characterization of the activity of the trans-aconitate methyltransferase from Saccharomyces cerevisiae. Biochemistry 40(45):13699-709 SGD PMID 11695919
- ↑ Katz JE, et al. (2004) 3-Isopropylmalate is the major endogenous substrate of the Saccharomyces cerevisiae trans-aconitate methyltransferase. Biochemistry 43(20):5976-86 SGD PMID 15147181
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