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Gene Review

glyA  -  serine hydroxymethyltransferase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK2548, JW2535
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Disease relevance of glyA


High impact information on glyA

  • From the genome analysis of the Mycobacterium tuberculosis two putative genes namely GlyA and GlyA2 have been proposed to encode for the enzyme serine hydroxymethyltransferase [6].
  • The results are discussed in terms of the role of each Pro residue in maintaining the structure and function of SHMT and a possible role in pyridoxal 5'-phosphate addition to the apo-enzyme [7].
  • Role of proline residues in the folding of serine hydroxymethyltransferase [7].
  • The 5 Pro residues were each mutated to both a Gly and Ala residue, and each mutant SHMT was purified and characterized with respect to kinetic properties, stability, secondary structure, and folding mechanism [7].
  • The first structure of the serine-bound form of SHMT allows identification of residues involved in serine binding and catalysis [8].

Chemical compound and disease context of glyA


Biological context of glyA


Anatomical context of glyA

  • A comparison of the site of each Tn5 insertion within the glyA gene or within gene X and the size of the polypeptide observed in the cell-free system enabled us to determine the direction of transcription and translation of both genes [17].
  • Serine hydroxymethyltransferase (SHMT) from plant mitochondria was shown to be inhibited by 5-CHO-H(4)PteGlu(n) as are SHMTs from other organisms [18].
  • Serine hydroxymethyltransferase purified from rabbit liver cytosol has at least two Asn residues (Asn(5) and Asn(220)) that are 67 and 30% deamidated, respectively [19].

Associations of glyA with chemical compounds

  • Activation of glyA by the MetR protein requires homocysteine, an intermediate in methionine biosynthesis [9].
  • The increase in SHMT activity was sufficient to correct the glycine auxotrophy of strains lacking folA [20].
  • The mutation responsible for these phenotypes mapped to the glyA gene, a biosynthetic gene encoding the enzyme that converts serine and tetrahydrofolate to glycine and 5,10-methylenetetrahydrofolate [21].
  • The glyA gene was identified on the insert by analyzing a set of plasmids derived from pGS1 that carry random insertions of the transposable kanamycin resistance element Tn5 [22].
  • The presence of hypoxanthine, the co-repressor of PurR, increases the ability of PurR to prevent RNAP binding, providing a model for repression of the glyA gene by PurR [23].

Other interactions of glyA


Analytical, diagnostic and therapeutic context of glyA


  1. A novel mechanism for upregulation of the Escherichia coli K-12 hmp (flavohaemoglobin) gene by the 'NO releaser', S-nitrosoglutathione: nitrosation of homocysteine and modulation of MetR binding to the glyA-hmp intergenic region. Membrillo-Hernández, J., Coopamah, M.D., Channa, A., Hughes, M.N., Poole, R.K. Mol. Microbiol. (1998) [Pubmed]
  2. Identification of glyA as a symbiotically essential gene in Bradyrhizobium japonicum. Rossbach, S., Hennecke, H. Mol. Microbiol. (1991) [Pubmed]
  3. Cloning and expression of the Campylobacter jejuni glyA gene in Escherichia coli. Chan, V.L., Bingham, H., Kibue, A., Nayudu, P.R., Penner, J.L. Gene (1988) [Pubmed]
  4. Cloning and characterization of the gene for Salmonella typhimurium serine hydroxymethyltransferase. Urbanowski, M.L., Plamann, M.D., Stauffer, L.T., Stauffer, G.V. Gene (1984) [Pubmed]
  5. Recombinant production of serine hydroxymethyl transferase from Streptococcus thermophilus and its preliminary evaluation as a biocatalyst. Vidal, L., Calveras, J., Clapés, P., Ferrer, P., Caminal, G. Appl. Microbiol. Biotechnol. (2005) [Pubmed]
  6. Unusual structural, functional, and stability properties of serine hydroxymethyltransferase from Mycobacterium tuberculosis. Chaturvedi, S., Bhakuni, V. J. Biol. Chem. (2003) [Pubmed]
  7. Role of proline residues in the folding of serine hydroxymethyltransferase. Fu, T.F., Boja, E.S., Safo, M.K., Schirch, V. J. Biol. Chem. (2003) [Pubmed]
  8. Crystal structure of binary and ternary complexes of serine hydroxymethyltransferase from Bacillus stearothermophilus: insights into the catalytic mechanism. Trivedi, V., Gupta, A., Jala, V.R., Saravanan, P., Rao, G.S., Rao, N.A., Savithri, H.S., Subramanya, H.S. J. Biol. Chem. (2002) [Pubmed]
  9. Regulation of the Escherichia coli glyA gene by the metR gene product and homocysteine. Plamann, M.D., Stauffer, G.V. J. Bacteriol. (1989) [Pubmed]
  10. Regulation of the Escherichia coli glyA gene by the purR gene product. Steiert, J.G., Rolfes, R.J., Zalkin, H., Stauffer, G.V. J. Bacteriol. (1990) [Pubmed]
  11. Threonine formation via the coupled activity of 2-amino-3-ketobutyrate coenzyme A lyase and threonine dehydrogenase. Marcus, J.P., Dekker, E.E. J. Bacteriol. (1993) [Pubmed]
  12. Sequence homology between prokaryotic and eukaryotic forms of serine hydroxymethyltransferase. Barra, D., Martini, F., Angelaccio, S., Bossa, F., Gavilanes, F., Peterson, D., Bullis, B., Schirch, L. Biochem. Biophys. Res. Commun. (1983) [Pubmed]
  13. Crystal structure at 2.4 A resolution of E. coli serine hydroxymethyltransferase in complex with glycine substrate and 5-formyl tetrahydrofolate. Scarsdale, J.N., Radaev, S., Kazanina, G., Schirch, V., Wright, H.T. J. Mol. Biol. (2000) [Pubmed]
  14. Role of MetR and PurR in the activation of glyA by CsgD in Escherichia coli K-12. Chirwa, N.T., Herrington, M.B. Can. J. Microbiol. (2004) [Pubmed]
  15. Complete nucleotide sequence of the E. coli glyA gene. Plamann, M.D., Stauffer, L.T., Urbanowski, M.L., Stauffer, G.V. Nucleic Acids Res. (1983) [Pubmed]
  16. Mutation that suppresses the protein export defect of the secY mutation and causes cold-sensitive growth of Escherichia coli. Shiba, K., Ito, K., Yura, T. J. Bacteriol. (1984) [Pubmed]
  17. Characterization of the Escherichia coli gene for serine hydroxymethyltransferase. Plamann, M.D., Stauffer, G.V. Gene (1983) [Pubmed]
  18. Cloning and characterization of mitochondrial 5-formyltetrahydrofolate cycloligase from higher plants. Roje, S., Janave, M.T., Ziemak, M.J., Hanson, A.D. J. Biol. Chem. (2002) [Pubmed]
  19. Deamidation of asparagine residues in a recombinant serine hydroxymethyltransferase. di Salvo, M.L., Delle Fratte, S., Maras, B., Bossa, F., Wright, H.T., Schirch, V. Arch. Biochem. Biophys. (1999) [Pubmed]
  20. CsgD, a regulator of curli and cellulose synthesis, also regulates serine hydroxymethyltransferase synthesis in Escherichia coli K-12. Chirwa, N.T., Herrington, M.B. Microbiology (Reading, Engl.) (2003) [Pubmed]
  21. Modulation of the heat shock response by one-carbon metabolism in Escherichia coli. Gage, D.J., Neidhardt, F.C. J. Bacteriol. (1993) [Pubmed]
  22. Construction and expression of hybrid plasmids containing the Escherichia coli glyA genes. Stauffer, G.V., Plamann, M.D., Stauffer, L.T. Gene (1981) [Pubmed]
  23. RNA polymerase, PurR and MetR interactions at the glyA promoter of Escherichia coli. Lorenz, E., Stauffer, G.V. Microbiology (Reading, Engl.) (1996) [Pubmed]
  24. Escherichia coli glyA mRNA decay: the role of 3' secondary structure and the effects of the pnp and rnb mutations. Plamann, M.D., Stauffer, G.V. Mol. Gen. Genet. (1990) [Pubmed]
  25. Site-directed mutagenesis techniques in the study of Escherichia coli serine hydroxymethyltransferase. Iurescia, S., Condò, I., Angelaccio, S., Delle Fratte, S., Bossa, F. Protein Expr. Purif. (1996) [Pubmed]
  26. Properties of a serine hydroxymethyltransferase in which an active site histidine has been changed to an asparagine by site-directed mutagenesis. Hopkins, S., Schirch, V. J. Biol. Chem. (1986) [Pubmed]
  27. Diffraction grade crystals of Escherichia coli serine hydroxymethyltransferase. Stover, P., Kruschwitz, H., Schirch, V., Wright, H.T. J. Mol. Biol. (1993) [Pubmed]
  28. Molecular organization, catalytic mechanism and function of serine hydroxymethyltransferase--a potential target for cancer chemotherapy. Rao, N.A., Talwar, R., Savithri, H.S. Int. J. Biochem. Cell Biol. (2000) [Pubmed]
  29. Purification of serine hydroxymethyltransferase from Bacillus stearothermophilus with ion-exchange high-performance liquid chromatography. Ide, H., Hamaguchi, K., Kobata, S., Murakami, A., Kimura, Y., Makino, K., Kamáda, M., Miyamoto, S., Nagaya, T., Kamogawa, K. J. Chromatogr. (1992) [Pubmed]
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