EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
4.2.1.22 | S-adenosyl-L-methionine | the enzyme is allosterically activated by S-adenosyl-L-methionine under normal conditions but is destabilized under pathological conditions | Mus musculus | |
4.2.1.22 | S-adenosyl-L-methionine | the enzyme is allosterically activated by S-adenosyl-L-methionine under normal conditions but is destabilized under pathological conditions | Homo sapiens |
EC Number | General Stability | Organism |
---|---|---|
4.2.1.22 | binding of S-adenosyl-L-methionine stabilizes cystathionine beta-synthase against degradation. Under pathological conditions with reduced levels of S-adenosyl-L-methionine (human hepatocellular carcinoma), level of cystathionine beta-synthase is diminished. This decrease in cystathionine beta-synthase level correlates with reduced glutathione that is, in turn, associated with increased vulnerability to oxidative stress. Posttranslational regulation of cystathionine beta-synthase stability by S-adenosyl-L-methionine provides a mechanism for achieving coordinate changes in cellular methylation and antioxidant status that is observed in a number of disease states | Homo sapiens |
4.2.1.22 | binding of S-adenosyl-L-methionine stabilizes cystathionine beta-synthase against degradation. Under pathological conditions with reduced levels of S-adenosyl-L-methionine (mouse model for chronic steatohepatitis), level of cystathionine beta-synthase is diminished. This decrease in cystathionine beta-synthase level correlates with reduced glutathione that is, in turn, associated with increased vulnerability to oxidative stress. Posttranslational regulation of cystathionine beta-synthase stability by S-adenosyl-L-methionine provides a mechanism for achieving coordinate changes in cellular methylation and antioxidant status that is observed in a number of disease states | Mus musculus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.2.1.22 | L-serine + L-homocysteine | Mus musculus | - |
cystathionine + H2O | - |
? | |
4.2.1.22 | L-serine + L-homocysteine | Homo sapiens | - |
cystathionine + H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.2.1.22 | Homo sapiens | - |
- |
- |
4.2.1.22 | Mus musculus | - |
mouse model for spontaneous steatohepatitis in which the gene for the MAT1A isoenzyme encoding AdoMet synthetase has been disrupted | - |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
4.2.1.22 | hepatoma cell | reduced cystathionine beta-synthase | Homo sapiens | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.2.1.22 | L-serine + L-homocysteine | - |
Mus musculus | cystathionine + H2O | - |
? | |
4.2.1.22 | L-serine + L-homocysteine | - |
Homo sapiens | cystathionine + H2O | - |
? |