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Literature summary for 2.1.2.1 extracted from

  • Bhatt, A.N.; Bhakuni, V.; Kumar, A.; Khan, M.Y.; Siddiqi, M.I.
    Alkaline pH-dependent differential unfolding characteristics of mesophilic and thermophilic homologs of dimeric serine hydroxymethyltransferase (2010), Biochim. Biophys. Acta, 1804, 1294-1300.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and chimeric mutant in Escherichia coli strain BL21 (DE3) Bacillus subtilis
expression of wild-type and chimeric mutant in Escherichia coli strain BL21 (DE3) Geobacillus stearothermophilus

Protein Variants

Protein Variants Comment Organism
additional information generation of a chimera from Bacillus stearothermophilus and Bacillus subtilis SHMTs by domain swapping, quarternary structure analysis, overview Bacillus subtilis
additional information generation of a chimera from Bacillus stearothermophilus and Bacillus subtilis SHMTs by domain swapping, quarternary structure analysis, overview Geobacillus stearothermophilus

General Stability

General Stability Organism
bsSHMT has six unconserved lysine residues in C-terminal domain which render it more resistant to alkaline denaturation. Chemical modification of lysine side chains results in stabilization of monomers Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Geobacillus stearothermophilus
-
-
-

Subunits

Subunits Comment Organism
dimer homology modeling and comparison to SHMT from Bacillus stearothermophilus, using the crystal structure, PDB ID 1KKJ, overview Bacillus subtilis
dimer homology modeling using the crystal structure, PDB ID 1KKJ, and comparison to SHMT from Bacillus subtilis, overview Geobacillus stearothermophilus

Synonyms

Synonyms Comment Organism
serine hydroxymethyltransferase
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Bacillus subtilis
serine hydroxymethyltransferase
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Geobacillus stearothermophilus
SHMT
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Bacillus subtilis
SHMT
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Geobacillus stearothermophilus

pH Stability

pH Stability pH Stability Maximum Comment Organism
additional information
-
recombinant wild-type bsSHMT and chimeric mutant enzyme are significantly higher susceptible to proteolysis into smaller protein fragments at pH 11 as compared to neutral pH Bacillus subtilis
additional information
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recombinant wild-type bstSHMT and chimeric mutant enzyme are only merginally susceptible to proteolysis into smaller protein fragments at pH 11 and at neutral pH Geobacillus stearothermophilus