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Literature summary for 4.2.1.22 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
Search for more literature for 4.2.1.22

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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 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]

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