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Literature summary for 2.5.1.47 extracted from

  • Matoba, Y.; Yoshida, T.; Izuhara-Kihara, H.; Noda, M.; Sugiyama, M.
    Crystallographic and mutational analyses of cystathionine beta-synthase in the H2S-synthetic gene cluster in Lactobacillus plantarum (2017), Protein Sci., 26, 763-783 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
to 2.4 A resolution Lactiplantibacillus plantarum

Protein Variants

Protein Variants Comment Organism
A70S residue at the substrate binding pocket, important for the H2S-generating activity Lactiplantibacillus plantarum
E223G residue at the substrate binding pocket, important for the H2S-generating activity Lactiplantibacillus plantarum

Organism

Organism UniProt Comment Textmining
Lactiplantibacillus plantarum F9UT54 bifunctional cystathionine beta-synthase EC 4.2.1.22 and O-acetyl-L-serine sulfhydrylase, EC 2.5.1.47
-
Lactiplantibacillus plantarum ATCC BAA-793 F9UT54 bifunctional cystathionine beta-synthase EC 4.2.1.22 and O-acetyl-L-serine sulfhydrylase, EC 2.5.1.47
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 L-cysteine
-
Lactiplantibacillus plantarum (2R,2'R)-3,3'-sulfanediylbis(2-aminopropanoic acid) + H2S
-
?
L-cysteine + L-homocysteine
-
Lactiplantibacillus plantarum L-cystathionine + H2S
-
?
O-acetyl-L-serine
-
Lactiplantibacillus plantarum L-cysteine + acetate
-
?
O-acetyl-L-serine + H2O
-
Lactiplantibacillus plantarum pyruvate + acetate + NH3
-
?
O-acetyl-L-serine + L-homocysteine
-
Lactiplantibacillus plantarum cystathionine + acetate
-
?