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Literature summary extracted from
- Properties of an unusual heme cofactor in PLP-dependent cystathionine beta-synthase (2007), Nat. Prod. Rep., 24, 631-639.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.1.22 | carbon monoxide | - |
Homo sapiens |  |
| 4.2.1.22 | nitric oxide | - |
Homo sapiens | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.2.1.22 | Homo sapiens | P35520 | - |
- |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.1.22 | 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 | |
| 4.2.1.22 | pyridoxal 5'-phosphate | - |
Homo sapiens | |
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Release 2023.1 (January 2023)
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