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Literature summary extracted from

  • Prudova, A.; Bauman, Z.; Braun, A.; Vitvitsky, V.; Lu, S.C.; Banerjee, R.
    S-adenosylmethionine stabilizes cystathionine beta-synthase and modulates redox capacity (2006), Proc. Natl. Acad. Sci. USA, 103, 6489-6494.
    View publication on PubMedView publication on EuropePMC

Activating Compound

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

General Stability

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

Natural Substrates/ Products (Substrates)

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
-
?

Organism

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
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.2.1.22 hepatoma cell reduced cystathionine beta-synthase Homo sapiens
-

Substrates and Products (Substrate)

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
-
?