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Literature summary for 4.2.1.22 extracted from

  • Tu, Y.; Kreinbring, C.A.; Hill, M.; Liu, C.; Petsko, G.A.; McCune, C.D.; Berkowitz, D.B.; Liu, D.; Ringe, D.
    Crystal structures of cystathionine beta-synthase from Saccharomyces cerevisiae One enzymatic step at a time (2018), Biochemistry, 57, 3134-3145 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P32582
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Synonyms

Synonyms Comment Organism
Cys4
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Saccharomyces cerevisiae

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
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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