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Literature summary extracted from

  • Hnizda, A.; Spiwok, V.; Jurga, V.; Kozich, V.; Kodicek, M.; Kraus, J.P.
    Cross-talk between the catalytic core and the regulatory domain in cystathionine beta-synthase: study by differential covalent labeling and computational modeling (2010), Biochemistry, 49, 10526-10534.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.2.1.22 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(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.22 expression of mutant 45CBS and wild-type CBS in Escherichia coli Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.22 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.1.22 61000
-
 4 * 61000 Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.22 L-serine + L-homocysteine Homo sapiens
-
 L-cystathionine + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.22 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.22 recombinant mutant 45CBS and wild-type CBS from Escherichia coli to homogeneity Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.22 L-serine + L-homocysteine
-
 Homo sapiens L-cystathionine + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.22 homotetramer 4 * 61000 Homo sapiens
4.2.1.22 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

EC Number Synonyms Comment Organism
4.2.1.22 CBS
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.1.22 additional information
-
 wild-type CBS is therminally activated at 55°C Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
4.2.1.22 pyridoxal 5'-phosphate
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
4.2.1.22 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
4.2.1.22 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
4.2.1.22 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
4.2.1.22 physiological function regulation mechanisms, overview Homo sapiens