| Gene Symbol | CBS |
| Aliases | CBSPROTEIN |
| Function | Cystathionine Beta Synthase (CBS) is a pyridoxal phosphate (PLP)-dependent enzyme that catalyzes the condensation of serine and homocysteine to form cystathionine, a critical intermediate in the tr... |
| Subcellular Localization | </strong></td><td>Cytoplasm, Mitochondria</td></tr> |
| GeneCards | CBS |
| Human Protein Atlas | CBS |
| Dimeric assembly | Each monomer contains N-terminal catalytic and C-terminal regulatory domains |
| Tetramer formation | Dimers can further associate into tetramers, enhancing stability |
| Allosteric regulation | SAM binding to C-terminal domains propagates conformational changes to the catalytic site |
| Active site geometry | The PLP Schiff base is positioned for optimal catalysis with substrates |
| S-adenosylmethionine (SAM) binding | Primary allosteric activator |
| S-adenosylhomocysteine (SAH) inhibition | Product inhibitor |
| Heme binding | Stabilizes the protein structure |
| Oxidative modifications | Reactive oxygen species can inhibit activity |
| Phosphorylation | Several kinases may regulate CBS activity |
| Databases | GeneCardsUniProtNCBI GeneHPASTRING |
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