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Cystathionine beta synthase (CBS) is involved in oocyte development. However, little is known about the regional and cellular expression patterns of CBS in the ovary and research is now focused on determining the location and expression during follicle development in the ovaries.
In molecular biology, the CBS domain is a protein domain found in a range of proteins in all species from bacteria to humans. It was first identified as a conserved sequence region in 1997 and named after cystathionine beta synthase, one of the proteins it is found in. [2] CBS domains are also found in a wide variety of other proteins such as inosine monophosphate dehydrogenase, [3] voltage ...
Ovarian cancer has a significant effect on quality of life, psychological health and well-being. Interventions are available to help with the needs and social support. Many ovarian cancer survivors report a good quality of life and optimism. Others reported a "spiritual change" that helped them find meaning during their experience. Others have ...
Cystathionine is an intermediate in the synthesis of cysteine from homocysteine. It is produced by the transsulfuration pathway and is converted into cysteine by cystathionine gamma-lyase (CTH). Biosynthetically, cystathionine is generated from homocysteine and serine by cystathionine beta synthase (upper reaction in the diagram below).
Cystathionine beta-lyase (EC 4.4.1.8), also commonly referred to as CBL or β-cystathionase, is an enzyme that primarily catalyzes the following α,β-elimination reaction [1] Reaction catalyzed by cystathionine beta-lyase. Thus, the substrate of this enzyme is L-cystathionine, whereas its 3 products are homocysteine, pyruvate, and ammonia. [2 ...
Reaction 5 is catalyzed by cystathionine beta-synthase while reaction 6 is catalyzed by cystathionine gamma-lyase. The required homocysteine is synthesized from methionine in reactions 1, 2, and 3. The transsulfuration pathway is a metabolic pathway involving the interconversion of cysteine and homocysteine through the intermediate cystathionine.
Cystathionine γ-lyase (no common gene name) which joins an activated serine ester (acetyl or succinyl) with homocysteine to form cystathionine; Not Cystathionine β-synthase which is a PLP enzyme type II; cysteine biosynthesis from serine: O-acetyl serine sulfhydrylase (cysK or cysM) which adds a thiol group to an activated serine ester
Other members include cystathionine γ synthase, cystathionine β lyase, and methionine γ lyase. [8] It is also a member of the broader aspartate aminotransferase family. [1] [8] Like many other PLP-dependent enzymes, cystathionine γ-lyase is a tetramer with D2 symmetry. [8] Pyridoxal phosphate is bound in the active site by Lys 212. [2]