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Literature summary for 4.2.1.22 extracted from

  • Singh, S.; Ballou, D.; Banerjee, R.
    Pre-steady-state kinetic analysis of enzyme-monitored turnover during cystathionine beta-synthase-catalyzed H2S generation (2011), Biochemistry, 50, 419-425.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.2.1.22

Cloned(Commentary)

Cloned (Comment) Organism
expression of cystathionine beta-synthase in Escherichia coli strain BL21(DE3) Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information pre-steady-state kinetic analysis of enzyme-monitored turnover during cystathionine beta-synthase-catalyzed H2S generation, overview Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
55000
-
 x * 55000, SDS-PAGE Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-serine + L-homocysteine Saccharomyces cerevisiae
-
 L-cystathionine + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant cystathionine beta-synthase from Escherichia coli strain BL21(DE3) by anion exchange and hydroxyapatite chromatography Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-serine + L-homocysteine
-
 Saccharomyces cerevisiae L-cystathionine + H2O
-
 ?
additional information cystathionine beta-synthase also catalyze H2S production. The most efficient route for H2S generation by cystathionine beta-synthase is the beta-replacement of the cysteine thiol with homocysteine. In this reaction, cystathionine beta-synthase first reacts with cysteine to release H2S and forms an aminoacrylate intermediate. Homocysteine binds to the E 3 aminoacrylate intermediate with a bimolecular rate constant of 142 mM/s and rapidly condenses to form the enzyme-bound external aldimine of cystathionine. The reactions could be partially rate limited by release of the products, cystathionine and H2S Saccharomyces cerevisiae ?
-
 ?

Subunits

Subunits Comment Organism
? x * 55000, SDS-PAGE Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
yCBS
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 cystathionine beta-synthase assay at Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information the kcat for the generation of H2S by cystathionine beta-synthase of 55/s at 37°C, via the condensation of cysteine and homocysteine is 18fold faster than that for the beta-elimination and rehydration to form serine of 3/s- Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 cystathionine beta-synthase assay at Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
additional information yeast cystathionine beta-synthase does not have a heme cofactor Saccharomyces cerevisiae
pyridoxal 5'-phosphate
-
 Saccharomyces cerevisiae

General Information

General Information Comment Organism
evolution cystathionine beta-synthase belongs to the fold II family of pyridoxal 5'-phosphate enzymes Saccharomyces cerevisiae
metabolism cystathionine beta-synthase catalyzes the first step in the transsulfuration pathway in mammals, i.e. the condensation of serine and homocysteine to produce cystathionine and water Saccharomyces cerevisiae