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

BRENDA support

Literature summary extracted from

  • Mino, K.; Ishikawa, K.
    Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1 (2003), J. Bacteriol., 185, 2277-2284.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.47 expression in Escherichia coli Aeropyrum pernix
2.5.1.65 expression in Escherichia coli Rosetta (DE3), sequencing Aeropyrum pernix

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.47 21
-
 thiosulfate synthesis of S-sulfo-L-cysteine Aeropyrum pernix
2.5.1.47 24
-
 O-acetyl-L-Ser synthesis of S-sulfo-L-cysteine Aeropyrum pernix
2.5.1.47 28
-
 O-acetyl-L-Ser sulfhydrylation of O-acetyl-L-serine Aeropyrum pernix
2.5.1.65 additional information
-
 additional information
-
 Aeropyrum pernix
2.5.1.65 0.2
-
 Sulfide below, pH 6.7 Aeropyrum pernix
2.5.1.65 28
-
 O-acetyl-L-serine pH 6.7 Aeropyrum pernix

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.5.1.47 42000
-
 2 * 42000, SDS-PAGE Aeropyrum pernix
2.5.1.47 70580
-
 sedimentation equilibrium Aeropyrum pernix
2.5.1.65 42000
-
 2 * 42000, SDS-PAGE Aeropyrum pernix
2.5.1.65 70580
-
 sedimentation equilibrium ultracentrifugation Aeropyrum pernix

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 Arabidopsis thaliana the cysteine synthase complex functions as a molecular sensor system that monitors the sulfur status of the cell and controls sulfate assimilation and cysteine synthesis according to the availability of sulfate L-Cys + acetate
-
 ?
2.5.1.65 additional information Aeropyrum pernix biosynthesis of L-cysteine ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.47 Aeropyrum pernix
-
 K1
-
2.5.1.47 Arabidopsis thaliana
-
-
-
2.5.1.65 Aeropyrum pernix
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.47
-
 Aeropyrum pernix
2.5.1.65 recombinant OASS Aeropyrum pernix

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 50.9
-
-
 Aeropyrum pernix
2.5.1.65 50.9
-
 pH 6.7, 60°C, O-acetyl-L-serine sulfhydrylation Aeropyrum pernix

Storage Stability

EC Number Storage Stability Organism
2.5.1.65 4°C, enzyme solution, stable Aeropyrum pernix

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.47 L-cysteine + dithiothreitol
-
 Aeropyrum pernix S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
-
 ?
2.5.1.47 L-homocysteine + L-serine
-
 Aeropyrum pernix L-cystathionine + H2O
-
 ?
2.5.1.47 O-acetyl-L-Ser + H2S
-
 Arabidopsis thaliana L-Cys + acetate
-
 ?
2.5.1.47 O-acetyl-L-Ser + H2S
-
 Aeropyrum pernix L-Cys + acetate
-
 ?
2.5.1.47 O-acetyl-L-Ser + sulfide the cysteine synthase complex functions as a molecular sensor system that monitors the sulfur status of the cell and controls sulfate assimilation and cysteine synthesis according to the availability of sulfate Arabidopsis thaliana L-Cys + acetate
-
 ?
2.5.1.47 O-acetyl-L-Ser + thiosulfate
-
 Aeropyrum pernix S-sulfocysteine + sodium acetate
-
 ?
2.5.1.47 O-acetyl-L-serine
-
 Aeropyrum pernix L-cysteine + acetate
-
 ?
2.5.1.65 L-cysteine + dithiothreitol OASS has a high activity in the L-cysteine desulfurization reaction Aeropyrum pernix S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + sulfide
-
 ?
2.5.1.65 additional information biosynthesis of L-cysteine Aeropyrum pernix ?
-
 ?
2.5.1.65 additional information enzyme with cystathionine beta-synthase and O-acetylserine sulfhydrylase activity in vitro, OASS has also L-serine sulfhydrylation and S-sulfo-L-cysteine synthesis activity Aeropyrum pernix ?
-
 ?
2.5.1.65 O-acetyl-L-serine + sulfide
-
 Aeropyrum pernix L-cysteine + acetic acid
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.47 dimer
-
 Arabidopsis thaliana
2.5.1.47 dimer 2 * 42000, SDS-PAGE Aeropyrum pernix
2.5.1.65 dimer 2 * 42000, SDS-PAGE Aeropyrum pernix

Synonyms

EC Number Synonyms Comment Organism
2.5.1.65 APE1586 Aeropyrum pernix K1, open reading frame Aeropyrum pernix
2.5.1.65 O-acetylserine sulfhydrylase
-
 Aeropyrum pernix
2.5.1.65 OASS
-
 Aeropyrum pernix

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.5.1.47 70
-
 maximal for O-acetyl-L-serine sulfhydrylation at both 70°C and at 80°C Aeropyrum pernix
2.5.1.47 80
-
 synthesis of L-cystathionine and sulfhydrylation of L-Ser. Maximal for O-acetyl-L-serine sulfhydrylation at both 70°C and at 80°C Aeropyrum pernix
2.5.1.47 90
-
 synthesis of S-sulfo-L-cysteine Aeropyrum pernix

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.5.1.47 100
-
 pH 6.1 and 6.7, 6 h, 10% loss of activity Aeropyrum pernix
2.5.1.65 100
-
 6 h, pH 6.1 and 6.7: 10% loss of activity, pH 7.5: 44% loss of activity, pH 8.5: 89% loss of activity Aeropyrum pernix

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.5.1.47 24
-
 thiosulfate synthesis of S-sulfo-L-cysteine Aeropyrum pernix
2.5.1.47 24
-
 O-acetyl-L-Ser synthesis of S-sulfo-L-cysteine Aeropyrum pernix
2.5.1.47 202
-
 H2S sulfhydrylation of O-acetyl-L-serine Aeropyrum pernix
2.5.1.47 202
-
 O-acetyl-L-Ser sulfhydrylation of O-acetyl-L-serine Aeropyrum pernix
2.5.1.65 additional information
-
 additional information
-
 Aeropyrum pernix
2.5.1.65 202
-
 O-acetyl-L-serine pH 6.7 Aeropyrum pernix

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.47 6.7
-
 sulfhydrylation of O-acetyl-L-serine Aeropyrum pernix
2.5.1.47 8.1 8.8 synthesis of L-cystathionine Aeropyrum pernix
2.5.1.65 6.7
-
-
 Aeropyrum pernix

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
2.5.1.65 6.1
-
 6 h, 100°C, 10% loss of activity Aeropyrum pernix
2.5.1.65 6.7
-
 6 h, 100°C, 10% loss of activity Aeropyrum pernix
2.5.1.65 7.5
-
 6 h, 100°C, 44% loss of activity Aeropyrum pernix
2.5.1.65 8.5
-
 6 h, 100°C, 89% loss of activity Aeropyrum pernix

Cofactor

EC Number Cofactor Comment Organism Structure
2.5.1.47 pyridoxal 5'-phosphate
-
 Arabidopsis thaliana
2.5.1.47 pyridoxal 5'-phosphate enzyme contains 1.2 pyridoxal phosphate per subunit Aeropyrum pernix
2.5.1.65 pyridoxal 5'-phosphate OASS contains 1.2 molecules pyridoxal 5'-phosphate per subunit, enzyme forms a Schiff base with pyridoxal 5'-phosphate Aeropyrum pernix