Activating Compound | Comment | Organism | Structure |
---|---|---|---|
S-adenosyl-L-methionine | allosteric activator. Binding of AdoMet to wild-type CBS moderately increases the protein stability toward urea, while it does not influence the unfolding cooperativity | Homo sapiens |
Cloned (Comment) | Organism |
---|---|
expression of mutant 45CBS and wild-type CBS in Escherichia coli | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
additional information | generation of a truncated 45 kDa CBS, 45CBS, enzyme lacking the C-terminal regulatory domain, amino acids 1-413. The wild-type CBS exhibits lower resistance to urea-induced denaturation and lower degree of unfolding cooperativity compared to 45CBS. Proteolytic kinetics by thermolysin under native conditions reveals slower cleavage of wild-type CBS compared to the mutant 45CBS | Homo sapiens |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
61000 | - |
4 * 61000 | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-serine + L-homocysteine | Homo sapiens | - |
L-cystathionine + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant mutant 45CBS and wild-type CBS from Escherichia coli to homogeneity | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-serine + L-homocysteine | - |
Homo sapiens | L-cystathionine + H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
homotetramer | 4 * 61000 | Homo sapiens |
More | CBS protein comprises three regions: the N-terminal heme-binding domain, residues 1-69, a highly conserved catalytic core, residues 70-413, and the C-terminal regulatory domain, resdiues 414-551, and an autoinhibitory module with binding site for the allosteric activator, S-adenosyl-L-methionine. Computational modeling of CBS structure, the enzyme has a regulatory dimer-dimer interface, homology modeling and protein-protein docking, overview. Model of wild-type CBS dimer by docking of a single C-terminal regulatory domain to mutant 45CBS dimer, PDB ID 1JBQ, and surface mapping of wild-type CBS and mutant 45CBS with diverse differentially reactive amino acid residues involved in conformational changes and thermal activation, overview | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
CBS | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
wild-type CBS is therminally activated at 55°C | Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
malfunction | CBS deficiency due to missense mutations in the CBS gene is the most common cause of inherited homocystinuria, a treatable multisystemic disease affecting to various extent vasculature, connective tissues, and central nervous system | Homo sapiens |
metabolism | cystathionine beta-synthase is a pyridoxal 5'-phosphate-dependent enzyme, which catalyzes the first step of the transsulfuration pathway, namely, the condensation of serine with homocysteine to cystathionine | Homo sapiens |
additional information | CBS is a modular enzyme, cross-talk between the catalytic core and the regulatory domain in cystathionine beta-synthase: study by differential covalent labeling and computational modeling, overview | Homo sapiens |
physiological function | regulation mechanisms, overview | Homo sapiens |