Difference between revisions of "YER175C"
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− | '''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=' | + | '''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='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|S000076422}} PMID 15147181</ref><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| | + | {{SGDpaper|S000066185}} PMID 11695919</ref> |
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Revision as of 13:05, 16 January 2009
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Systematic name | YER175C |
Gene name | TMT1 |
Aliases | TAM1 |
Feature type | ORF, Verified |
Coordinates | Chr V:540358..539459 |
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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- ↑ 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
- ↑ 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
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