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Literature summary for 4.2.1.22 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
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Activating Compound

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
95% purity Saccharomyces cerevisiae

Reaction

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

Substrates and Products (Substrate)

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