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Literature summary extracted from

  • Weeks, C.L.; Singh, S.; Madzelan, P.; Banerjee, R.; Spiro, T.G.
    Heme regulation of human cystathionine beta-synthase activity: insights from fluorescence and Raman spectroscopy (2009), J. Am. Chem. Soc., 131, 12809-12816.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.22 truncated protein lacking the C-terminal domain is expressed Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.22 DELTAC studies are carried out using a truncated protein lacking the C-terminal domain. kcat increases by a factor of 4 and the responsiveness to S-adenosyl-L-methionine is lost. The C-terminal domain is involved in the aggregation of the full-length protein, which exists as a mixture of tetramer and higher oligomers, while the 45 kDa truncated form lacking the C-terminal domain is a dimer Homo sapiens
4.2.1.22 R266M enzyme is inactivated, pyridoxal 5'-phosphate is displaced by breaking the salt bridge between Cys52 and Arg266 Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.22 CO CO binding is found to induce a tautomeric shift of the pyridoxal 5'-phosphate from the ketoenamine to the enolimine form. The ketoenamine is key to pyridoxal 5'-phosphate reactivity because its imine C-N bond is protonated, facilitating attack by the nucleophilic substrate, serine Homo sapiens
4.2.1.22 NO
-
 Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.1.22 45000
-
 molecular weight of the truncated protein lacking the C-terminal domain Homo sapiens

Organism

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

Subunits

EC Number Subunits Comment Organism
4.2.1.22 dimer
-
 Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
4.2.1.22 CBS
-
 Homo sapiens
4.2.1.22 cystathionine beta-synthase
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
4.2.1.22 heme CO binding displaces Cys52 from the heme Homo sapiens
4.2.1.22 pyridoxal 5'-phosphate
-
 Homo sapiens