Cystathionine Beta Synthase
Gene Ontology | |
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Molecular function | • cystathionine beta-synthase activity • protein binding • enzyme binding • heme binding • pyridoxal phosphate binding • ubiquitin protein ligase binding • protein homodimerization activity • metal ion binding • modified amino acid binding |
Cellular component | • nucleus • nucleolus • cytosol • intracellular membrane-bounded organelle |
Biological process | • sulfur amino acid metabolic process • endochondral ossification • blood vessel remodeling • cysteine biosynthetic process from serine • L-serine metabolic process • L-serine catabolic process • superoxide metabolic process • cysteine biosynthetic process via cystathionine • transsulfuration • L-cysteine catabolic process • cerebellum morphogenesis • regulation of cGMP metabolic process • cellular nitrogen compound metabolic process • homocysteine catabolic process • regulation of JUN kinase activity • small molecule metabolic process • homocysteine metabolic process • regulation of blood vessel size • response to folic acid • maternal process involved in female pregnancy • cartilage development involved in endochondral bone morphogenesis • hydrogen sulfide biosynthetic process |
Sources: Amigo / QuickGO |
44.47 – 44.5 Mb
31.61 – 31.64 Mb
Cystathionine-β-synthase, also known as CBS, is an enzyme (EC 4.2.1.22) that in humans is encoded by the CBS gene. It catalyzes the first step of the transsulfuration pathway, from homocysteine to cystathionine:
- L-serine + L-homocysteine L-cystathionine + H2O
CBS uses the cofactor pyridoxal-phosphate (PLP) and can be allosterically regulated by effectors such as the ubiquitous cofactor S-adenosyl-L-methionine (adoMet). This enzyme belongs to the family of lyases, to be specific, the hydro-lyases, which cleave carbon-oxygen bonds.
CBS is a multidomain enzyme composed of an N-terminal enzymatic domain and two CBS domains. The CBS gene is the most common locus for mutations associated with homocystinuria.
Read more about Cystathionine Beta Synthase: Nomenclature, Structure, Enzymatic Activity, Regulation, Human Disease, Bioengineering