Crystallization (Comment) | Organism |
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structure of the catalytic core, residues 1-353, to 1.5 A resolution, and structures with pyridoxal 5'-phosphate-L-serine external aldimine, aminoacrylate intermediate, cycloserine and hydrazine. Two monomers form a tight dimer. The monomer contains two structurally conserved salt bridges, residues E174/K42 and E44/R55, on the si side of the pyridoxal 5'-phosphate cofactor | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
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Saccharomyces cerevisiae | P32582 | - |
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Synonyms | Comment | Organism |
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Cys4 | - |
Saccharomyces cerevisiae |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
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additional information | - |
the CBS domain contributes only very little to the thermal stabilization of the enzyme. In the presence of 1 mM cycloserine, the full-length and catalytic-core enzymes are destabilized by 12 and 14.5°C, respectively | Saccharomyces cerevisiae |