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Gene Review

SHM1  -  glycine hydroxymethyltransferase SHM1

Saccharomyces cerevisiae S288c

Synonyms: Glycine hydroxymethyltransferase, SHMT, SHMT1, Serine hydroxymethyltransferase, mitochondrial, Serine methylase, ...
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High impact information on SHM1


Biological context of SHM1

  • The genes encoding both the cytosolic and mitochondrial serine hydroxymethyltransferases (SHM2 and SHM1, respectively) and a third unidentified gene of the yeast Saccharomyces cerevisiae have been isolated and their nucleotide sequences determined [2].
  • Lethality in the absence of the mitochondrial Shm1 and the cytoplasmic Ade3 enzymes indicates that, under certain circumstances, these cellular compartments cooperate in carrying out essential metabolic processes [3].
  • In vitro studies have considered the kinetics of the C1-THF synthase/SHMT enzyme system in the catalytic conversion of formate to serine [Strong et al. (1987) J. Biol. Chem. 262, 12519-12525] [4].

Anatomical context of SHM1


Associations of SHM1 with chemical compounds

  • Gene disruption studies demonstrated that inactivation of SHM1, SHM2, and GLY1 is required to yield yeast that are completely auxotrophic for glycine [2].
  • With the inactivation of SHM1, however, the glycine cleavage system can make an observable contribution to the level of mitochondrial formate [5].
  • Genes encoding the mitochondrial (SHM1) and cytosolic (SHM2) serine hydroxymethyltransferases, and the L-threonine aldolase gene (GLY1) from Candida albicans were cloned and sequenced [6].
  • Growth experiments using glucose as the sole carbon source showed that GLY1 is more important for glycine biosynthesis than SHM1 and SHM2 encoding alternative serine hydroxymethyltransferases [7].
  • However, when both serine and glycine were present, the mitochondrial SHMT made a significant contribution of one-carbon units, but not glycine, for purine synthesis [8].

Other interactions of SHM1

  • We report that mutations in the HIP1 and SHM1 genes exhibit synthetic lethality with ade3 deletions [3].
  • Growth of shm1 shm2 mutants was stimulated by glycine, whereas glycine could not supplement the growth of the isogenic gcv1 strain [9].


  1. Influence of the nuclear gene tmp3 on the loss of mitochondrial genes in Saccharomyces cerevisiae. Zelikson, R., Luzzati, M. Mol. Cell. Biol. (1982) [Pubmed]
  2. Cloning and molecular characterization of three genes, including two genes encoding serine hydroxymethyltransferases, whose inactivation is required to render yeast auxotrophic for glycine. McNeil, J.B., McIntosh, E.M., Taylor, B.V., Zhang, F.R., Tang, S., Bognar, A.L. J. Biol. Chem. (1994) [Pubmed]
  3. Pitfalls of the synthetic lethality screen in Saccharomyces cerevisiae: an improved design. Koren, A., Ben-Aroya, S., Steinlauf, R., Kupiec, M. Curr. Genet. (2003) [Pubmed]
  4. Whole-cell detection by 13C NMR of metabolic flux through the C1-tetrahydrofolate synthase/serine hydroxymethyltransferase enzyme system and effect of antifolate exposure in Saccharomyces cerevisiae. Pasternack, L.B., Laude, D.A., Appling, D.R. Biochemistry (1994) [Pubmed]
  5. In vivo analysis of folate coenzymes and their compartmentation in Saccharomyces cerevisiae. McNeil, J.B., Bognar, A.L., Pearlman, R.E. Genetics (1996) [Pubmed]
  6. Glycine metabolism in Candida albicans: characterization of the serine hydroxymethyltransferase (SHM1, SHM2) and threonine aldolase (GLY1) genes. McNeil, J.B., Flynn, J., Tsao, N., Monschau, N., Stahmann, K., Haynes, R.H., McIntosh, E.M., Pearlman, R.E. Yeast (2000) [Pubmed]
  7. Identification of Saccharomyces cerevisiae GLY1 as a threonine aldolase: a key enzyme in glycine biosynthesis. Monschau, N., Stahmann, K.P., Sahm, H., McNeil, J.B., Bognar, A.L. FEMS Microbiol. Lett. (1997) [Pubmed]
  8. Role of mitochondrial and cytoplasmic serine hydroxymethyltransferase isozymes in de novo purine synthesis in Saccharomyces cerevisiae. Kastanos, E.K., Woldman, Y.Y., Appling, D.R. Biochemistry (1997) [Pubmed]
  9. Cloning, and molecular characterization of the GCV1 gene encoding the glycine cleavage T-protein from Saccharomyces cerevisiae. McNeil, J.B., Zhang, F., Taylor, B.V., Sinclair, D.A., Pearlman, R.E., Bognar, A.L. Gene (1997) [Pubmed]
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