Protein Variants | Comment | Organism |
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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 | Organism |
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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 | UniProt | Comment | Textmining |
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Bacillus subtilis | - |
- |
- |
Geobacillus stearothermophilus | - |
- |
- |
Purification (Comment) | Organism |
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chimeric enzymes | Bacillus subtilis |
chimeric enzymes | Geobacillus stearothermophilus |
Subunits | Comment | Organism |
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dimer | - |
Bacillus subtilis |
dimer | - |
Geobacillus stearothermophilus |
Synonyms | Comment | Organism |
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bsSHMT | - |
Bacillus subtilis |
bstSHMT | - |
Geobacillus stearothermophilus |