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Literature summary extracted from

  • Taoka, S.; Banerjee, R.
    Stopped-flow kinetic analysis of the reaction catalyzed by the full-length yeast cystathionine beta-synthase (2002), J. Biol. Chem., 277, 22421-22425.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.1.22 1.2
-
 homocysteine 37°C, L-serine pre-treatment Saccharomyces cerevisiae
4.2.1.22 2.3
-
 homocysteine 37°C, homocysteine pre-treatment Saccharomyces cerevisiae
4.2.1.22 3.5
-
 L-serine 37°C, homocysteine pre-treatment Saccharomyces cerevisiae
4.2.1.22 4.9
-
 L-serine 37°C, L-serine pre-treatment Saccharomyces cerevisiae

Organism

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

Reaction

EC Number Reaction Comment Organism Reaction ID
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 in the forward direction an external aldimine of serine and an aminoacrylate intermediate are formed, the aminoacrylate binds to homocysteine and converts to cystathione, in the reverse reaction cystathione binds to the enzyme and is rapidly converted to the aminoacrylate without accumulation of the external aldimine Saccharomyces cerevisiae Cystathionine + H2O
-
 r

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.2.1.22 14.7
-
 L-serine 37°C, L-serine pre-treatment Saccharomyces cerevisiae
4.2.1.22 16.8
-
 L-serine 37°C, homocysteine pre-treatment Saccharomyces cerevisiae