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Literature summary for 2.1.2.1 extracted from

  • Bhatt, A.N.; Khan, M.Y.; Bhakuni, V.
    The C-terminal domain of dimeric serine hydroxymethyltransferase plays a key role in stabilization of the quaternary structure and cooperative unfolding of protein: domain swapping studies with enzymes having high sequence identity (2004), Protein Sci., 13, 2184-2195.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
additional information construction of chimeric enzymes by swapping the structural domains between the bsSHMT from Bacillus subtilis and the bstSHMT frok Bacillus stearothermophilus and generation of the two chimeric proteins bsbstc and bstbsc. The chimeras have secondary structure, tyrosine and pyridoxal 5'-phosphate microenvironment similar to that of the wild-type proteins. The chimeras show enzymatic activity slightly higher than that of the wild-type proteins.Unlike the wild-type enzyme bsSHMT, which undergoes dissociation of native dimer into monomers at low guanidinium chloride concentrations, resulting in a non-cooperative unfolding of the enzyme, its chimera bsbstc, having the C-terminal domain of bstSHMT is resistant to low guanidinium chloride concentration and shows a guanidinium-chloride-induced cooperative unfolding from native dimer to unfolded monomer. The wild-type dimeric bstSHMT is resistant to low guanidinium chloride concentrations and shows a guanidinium chloride-induced cooperative unfolding, whereas its chimera bstbsc, having the C-terminal domain of bsSHMT, shows dissociation of native dimer into monomer at low guanidinium chloride concentrations and a guanidinium-induced non-cooperative unfolding Bacillus subtilis
additional information construction of chimeric enzymes by swapping the structural domains between the bsSHMT from Bacillus subtilis and the bstSHMT from Bacillus stearothermophilus and generation of the two chimeric proteins bsbstc and bstbsc. The chimeras have secondary structure, tyrosine and pyridoxal 5'-phosphate microenvironment similar to that of the wild-type proteins. The chimeras show enzymatic activity slightly higher than that of the wild-type proteins.Unlike the wild-type enzyme bsSHMT, which undergoes dissociation of native dimer into monomers at low guanidinium chloride concentrations, resulting in a non-cooperative unfolding of the enzyme, its chimera bsbstc, having the C-terminal domain of bstSHMT is resistant to low guanidinium chloride concentration and shows a guanidinium-chloride-induced cooperative unfolding from native dimer to unfolded monomer. The wild-type dimeric bstSHMT is resistant to low guanidinium chloride concentrations and shows a guanidinium chloride-induced cooperative unfolding, whereas its chimera bstbsc, having the C-terminal domain of bsSHMT, shows dissociation of native dimer into monomer at low guanidinium chloride concentrations and a guanidinium-induced non-cooperative unfolding Geobacillus stearothermophilus

General Stability

General Stability Organism
unlike the wild-type enzyme bsSHMT, which undergoes dissociation of native dimer into monomers at low guanidinium chloride concentrations, resulting in a non-cooperative unfolding of the enzyme, its chimera bsbstc, having the C-terminal domain of bstSHMT is resistant to low guanidinium chloride concentration and shows a guanidinium-chloride-induced cooperative unfolding from native dimer to unfolded monomer. The wild-type dimeric bstSHMT is resistant to low guanidinium chloride concentrations and shows a guanidinium chloride-induced cooperative unfolding, whereas its chimera bstbsc, having the C-terminal domain of bsSHMT, shows dissociation of native dimer into monomer at low guanidinium chloride concentrations and a guanidinium-induced non-cooperative unfolding. The C-terminal domain of dimeric SHMT plays a vital role in stabilization of the oligomeric structure of the native enzyme hence modulating its unfolding pathway Bacillus subtilis
unlike the wild-type enzyme bsSHMT, which undergoes dissociation of native dimer into monomers at low guanidinium chloride concentrations, resulting in a non-cooperative unfolding of the enzyme, its chimera bsbstc, having the C-terminal domain of bstSHMT is resistant to low guanidinium chloride concentration and shows a guanidinium-chloride-induced cooperative unfolding from native dimer to unfolded monomer. The wild-type dimeric bstSHMT is resistant to low guanidinium chloride concentrations and shows a guanidinium chloride-induced cooperative unfolding, whereas its chimera bstbsc, having the C-terminal domain of bsSHMT, shows dissociation of native dimer into monomer at low guanidinium chloride concentrations and a guanidinium-induced non-cooperative unfolding. The C-terminal domain of dimeric SHMT plays a vital role in stabilization of the oligomeric structure of the native enzyme hence modulating its unfolding pathway Geobacillus stearothermophilus

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
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-
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Geobacillus stearothermophilus
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-
-

Purification (Commentary)

Purification (Comment) Organism
chimeric enzymes Bacillus subtilis
chimeric enzymes Geobacillus stearothermophilus

Subunits

Subunits Comment Organism
dimer
-
 Bacillus subtilis
dimer
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 Geobacillus stearothermophilus

Synonyms

Synonyms Comment Organism
bsSHMT
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 Bacillus subtilis
bstSHMT
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 Geobacillus stearothermophilus