EC Number   |
Cofactor |
Reference |
|---|
    4.2.1.22 | heme |
heme in CBS is six-coordinate, low spin, and contains cysteine and histidine as axial ligands, the unusual heme in CBS represents a potential source of cytosolic superoxide radical |
696253 |
| 4.2.1.22 | heme |
iron protoporphyrin IX |
650408 |
| 4.2.1.22 | heme |
requires a heme cofactor for maximal activity, heme plays a key role in proper CBS folding and assembly |
698850 |
| 4.2.1.22 | heme |
role of heme in cystathionine beta-synthase folding |
715808 |
| 4.2.1.22 | heme |
the heme favors the ferric state at lower pH and, in the presence of reductants, attains the ferric state via transient formation of the ferrous state. Fe(II)-enzyme and Fe(III)-enzyme are apparently interconverted by a proton-controlled internal electron transfer process |
664020 |
| 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 |
682076 |
| 4.2.1.22 | heme |
the specific activity of CBS improves 1.8-2.8fold under truncation of R51A and R224A when the heme iron is in the ferric state |
696822 |
| 4.2.1.22 | heme |
the specific activity of the alkaline form is approximately 25% of that for the intact CBS enzyme when the heme iron is in the ferric state |
697295 |
| 4.2.1.22 | heme |
vibrational coherence spectroscopy is used to probe the low-frequency vibrational motions of the heme and how they depend on structural distortions that are induced by the CBS protein environment |
705345 |
| 4.2.1.22 | more |
heme is no cofactor |
652551 |
