Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Chocat, P.; Esaki, N.; Tanaka, H.; Soda, K.
    Synthesis of selenocystine and selenohomocystine with O-acetylhomoserine sulfhydrylase (1985), Agric. Biol. Chem., 49, 1143-1150.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.49 Na2Se
-
 Saccharomyces cerevisiae
2.5.1.49 NaHS
-
 Saccharomyces cerevisiae
2.5.1.49 Se2-
-
 Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.49 0.52
-
 S2-
-
 Saccharomyces cerevisiae
2.5.1.49 0.7
-
 S2-
-
 Saccharomyces cerevisiae
2.5.1.49 1.2
-
 NaHSe L-serine-O-sulfate as acceptor Saccharomyces cerevisiae
2.5.1.49 2.5
-
 O-acetyl-L-serine NaHS as donor Saccharomyces cerevisiae
2.5.1.49 4
-
 L-serine-O-sulfate NaHS or Na2Se as donor Saccharomyces cerevisiae
2.5.1.49 4.1
-
 O-acetyl-L-homoserine NaHS as donor Saccharomyces cerevisiae
2.5.1.49 5
-
 O-acetyl-L-serine Na2Se as donor Saccharomyces cerevisiae
2.5.1.49 5.25
-
 O-acetyl-L-homoserine Na2Se as donor Saccharomyces cerevisiae
2.5.1.49 8.9
-
 Se2-
-
 Saccharomyces cerevisiae
2.5.1.49 10
-
 Na2Se L-serine-O-sulfate as acceptor Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.49 O-acetyl-L-homoserine + S2- Saccharomyces cerevisiae physiological substrate NaHS L-homocysteine + acetic acid
-
 ?
2.5.1.49 O-acetyl-L-serine + S2- Saccharomyces cerevisiae physiological substrate NaHS L-cysteine + acetic acid
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.49 Saccharomyces cerevisiae
-
 baker's yeast
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.49 partial Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.49 L-serine-O-sulfate + Na2Se
-
 Saccharomyces cerevisiae ?
-
 ?
2.5.1.49 L-serine-O-sulfate + NaHSe
-
 Saccharomyces cerevisiae ?
-
 ?
2.5.1.49 L-serine-O-sulfate + Se2-
-
 Saccharomyces cerevisiae L-selenocystine + ?
-
 ?
2.5.1.49 O-acetyl-L-homoserine + H2S
-
 Saccharomyces cerevisiae L-homocysteine + acetic acid
-
 ?
2.5.1.49 O-acetyl-L-homoserine + S2- physiological substrate NaHS Saccharomyces cerevisiae L-homocysteine + acetic acid
-
 ?
2.5.1.49 O-acetyl-L-homoserine + Se2-
-
 Saccharomyces cerevisiae L-selenohomocystine + ?
-
 ?
2.5.1.49 O-acetyl-L-serine + H2S
-
 Saccharomyces cerevisiae L-cysteine + acetic acid
-
 ?
2.5.1.49 O-acetyl-L-serine + NaHSe2
-
 Saccharomyces cerevisiae L-selenocystine + ?
-
 ?
2.5.1.49 O-acetyl-L-serine + S2- physiological substrate NaHS Saccharomyces cerevisiae L-cysteine + acetic acid
-
 ?
2.5.1.49 O-acetyl-L-serine + Se2-
-
 Saccharomyces cerevisiae L-selenocystine + ?
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.49 8
-
 optimum for gamma-replacement reaction of O-acetylhomoserine with Na2Se Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
2.5.1.49 pyridoxal 5'-phosphate
-
 Saccharomyces cerevisiae

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.5.1.49 22
-
 Se2-
-
 Saccharomyces cerevisiae
2.5.1.49 23
-
 Na2Se
-
 Saccharomyces cerevisiae
2.5.1.49 57
-
 NaHS O-acetlyhomoserine as substrate Saccharomyces cerevisiae
2.5.1.49 70
-
 NaHS L-serine-O-sulfate as substrate Saccharomyces cerevisiae