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Literature summary for 4.2.1.22 extracted from

  • Majtan, T.; Singh, L.R.; Wang, L.; Kruger, W.D.; Kraus, J.P.
    Active cystathionine beta-synthase can be expressed in heme-free systems in the presence of metal-substituted porphyrins or a chemical chaperone (2008), J. Biol. Chem., 283, 34588-34595.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
additional information treatment with 0.2 M trimethylamine-N-oxide results in rescuing expression as well as activity of CBS to 82% of human wild type CBS produced in a yeast heme-deficient strain Homo sapiens
S-adenosyl-L-methionine allosteric activation Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
expressed in heme-deficient strains of Saccharomyces cerevisiae and Escherichia coli Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
Co3+ Co3+ has 30-60% of the specific activity of Fe3+-CBS Homo sapiens
Mn3+ Mn3+ has 30-60% of the specific activity of Fe3+-CBS Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
glutathione-Sepharose column chromatography Homo sapiens

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
CBS
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
heme requires a heme cofactor for maximal activity, heme plays a key role in proper CBS folding and assembly Homo sapiens
pyridoxal 5'-phosphate dependent on Homo sapiens