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Literature summary extracted from

  • Yamagata, S.; Takeshima, K.
    O-Acetylserine and O-acetylhomoserine sulfhydrylase of yeast. Further purification and characterization as a pyridoxal enzyme (1976), J. Biochem., 80, 777-785.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.47 pyridoxal
-
 Saccharomyces cerevisiae
2.5.1.47 pyridoxal hydrochloride 54% inhibition at 1 mM Saccharomyces cerevisiae
2.5.1.49 pyridoxal inhibits the activity competitively with respect to pyridoxal 5'-phosphate Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.47 O-acetyl-L-Ser + sulfide Saccharomyces cerevisiae functions as a Cys synthase rather than as a homocysteine synthase in vivo L-Cys + acetate
-
 ?
2.5.1.49 O-acetyl-L-homoserine + H2S Saccharomyces cerevisiae
-
 L-homocysteine + acetic acid
-
 ?

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
2.5.1.49 urea denatured by 2.0 M urea Saccharomyces cerevisiae

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.47
-
 Saccharomyces cerevisiae
2.5.1.49
-
 Saccharomyces cerevisiae

Reaction

EC Number Reaction Comment Organism Reaction ID
2.5.1.47 O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate mechanism similar to those of other pyridoxal enzymes Saccharomyces cerevisiae
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.5.1.47 25.2
-
-
 Saccharomyces cerevisiae
2.5.1.49 25.2
-
-
 Saccharomyces cerevisiae

Storage Stability

EC Number Storage Stability Organism
2.5.1.47 -20 C, potassium phosphate buffer, pH 6.5, 1 mM EDTA, at least several days, no loss of activity Saccharomyces cerevisiae
2.5.1.49 -20°C, can be stored without any loss of activity Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.47 O-acetyl-L-Ser + sulfide functions as a Cys synthase rather than as a homocysteine synthase in vivo Saccharomyces cerevisiae L-Cys + acetate
-
 ?
2.5.1.49 O-acetyl-L-homoserine + H2S
-
 Saccharomyces cerevisiae L-homocysteine + acetic acid
-
 ?
2.5.1.49 O-acetyl-L-homoserine + methyl mercaptan
-
 Saccharomyces cerevisiae L-methionine + acetic acid
-
 ?
2.5.1.49 O-acetyl-L-serine + H2S
-
 Saccharomyces cerevisiae L-cysteine + acetic acid
-
 ?
2.5.1.49 O-acetyl-L-serine + methanethiol reaction only in phosphate buffer, relative activity compared to O-acetyl-L-homoserine 14.8% Saccharomyces cerevisiae ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.5.1.49 OAH
-
 Saccharomyces cerevisiae
2.5.1.49 OAS-OAH sulfhydrylase
-
 Saccharomyces cerevisiae

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.5.1.47 additional information
-
 pyridoxal 5'-phosphate stabilizes against heat inactivation Saccharomyces cerevisiae
2.5.1.47 55
-
 5 min, 45% loss of activity, without pyridoxal 5'-phosphate Saccharomyces cerevisiae
2.5.1.47 65
-
 5 min, complete loss of activity, without pyridoxal 5'-phosphate Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
2.5.1.47 pyridoxal 5'-phosphate stoichiometry, binds to Lys, protects against inactivation by heat, urea, and trypsin, four binding sites per mol apoenzyme, association constant Saccharomyces cerevisiae
2.5.1.49 pyridoxal 5'-phosphate
-
 Saccharomyces cerevisiae