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Literature summary extracted from

  • Kabil, O.; Toaka, S.; LoBrutto, R.; Shoemaker, R.; Banerjee, R.
    Pyridoxal phosphate binding sites are similar in human heme-dependent and yeast heme-independent cystathionine beta-synthases. Evidence from 31P NMR and pulsed EPR spectroscopy that heme and PLP cofactors are not proximal in the human enzyme (2001), J. Biol. Chem., 276, 19350-19355.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.2.1.22 heme regulatory role Homo sapiens
4.2.1.22 additional information enzyme is not dependent on heme Saccharomyces cerevisiae
4.2.1.22 pyridoxal 5'-phosphate
-
 Homo sapiens
4.2.1.22 pyridoxal 5'-phosphate
-
 Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.22 Homo sapiens
-
-
-
4.2.1.22 Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.22 95% purity Saccharomyces cerevisiae

Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.1.22 L-serine + L-homocysteine = L-cystathionine + H2O mechanism Homo sapiens
a
4.2.1.22 L-serine + L-homocysteine = L-cystathionine + H2O mechanism Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.22 L-Serine + homocysteine
-
 Homo sapiens Cystathionine + H2O
-
 r
4.2.1.22 L-Serine + homocysteine
-
 Saccharomyces cerevisiae Cystathionine + H2O
-
 r