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='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
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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='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
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  {{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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  1. 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
  2. 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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