3g5t

Structural highlights

Function

TMT1_YEAST Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate and 3-isopropylmalate at high affinity and of other molecules like cis-aconitate, isocitrate, and citrate at lower velocities and affinities. The function of trans-aconitate methylation appears to be in reducing the toxicity of this spontaneous breakdown product of cis-aconitate. The role of 3-isopropylmalate methylation is unclear but may represent a metabolic branch at 3-isopropylmalate, where some of the material is taken in the pathway leading to leucine and some is taken in a pathway to the 3-isopropylmalate methyl ester, a molecule that provides a signal to switch from vegetative to invasive growth in response to amino acid starvation.^{[1] [2] [3]}

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

1. ↑ Cai H, Dumlao D, Katz JE, Clarke S. Identification of the gene and characterization of the activity of the trans-aconitate methyltransferase from Saccharomyces cerevisiae. Biochemistry. 2001 Nov 13;40(45):13699-709. PMID:11695919
2. ↑ Katz JE, Dumlao DS, Wasserman JI, Lansdown MG, Jung ME, Faull KF, Clarke S. 3-Isopropylmalate is the major endogenous substrate of the Saccharomyces cerevisiae trans-aconitate methyltransferase. Biochemistry. 2004 May 25;43(20):5976-86. PMID:15147181 doi:http://dx.doi.org/10.1021/bi049784+
3. ↑ Dumlao DS, Hertz N, Clarke S. Secreted 3-isopropylmalate methyl ester signals invasive growth during amino acid starvation in Saccharomyces cerevisiae. Biochemistry. 2008 Jan 15;47(2):698-709. Epub 2007 Dec 20. PMID:18092814 doi:http://dx.doi.org/10.1021/bi7018157