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Literature summary for 4.2.1.22 extracted from

  • Singh, S.; Madzelan, P.; Banerjee, R.
    Properties of an unusual heme cofactor in PLP-dependent cystathionine beta-synthase (2007), Nat. Prod. Rep., 24, 631-639.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
carbon monoxide
-
Homo sapiens
nitric oxide
-
Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P35520
-
-

Cofactor

Cofactor Comment Organism Structure
heme the in vitro activity of cystathionine beta-synthase is sensitive to the redox state of the heme and is higher in the ferric form. Both carbon monoxide and nitric oxide bind to ferrous heme and inhibit the enzyme. The crystal structure of the protein reveals that the heme is about 20 A away from the active site Homo sapiens
pyridoxal 5'-phosphate
-
Homo sapiens