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Literature summary for 2.5.1.47 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
Search for more literature for 2.5.1.47

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Aeropyrum pernix

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
21
-
 thiosulfate synthesis of S-sulfo-L-cysteine Aeropyrum pernix
24
-
 O-acetyl-L-Ser synthesis of S-sulfo-L-cysteine Aeropyrum pernix
28
-
 O-acetyl-L-Ser sulfhydrylation of O-acetyl-L-serine Aeropyrum pernix

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
-
 ?

Organism

Organism UniProt Comment Textmining
Aeropyrum pernix
-
 K1
-
Arabidopsis thaliana
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Aeropyrum pernix

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
50.9
-
-
 Aeropyrum pernix

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-cysteine + dithiothreitol
-
 Aeropyrum pernix S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
-
 ?
L-homocysteine + L-serine
-
 Aeropyrum pernix L-cystathionine + H2O
-
 ?
O-acetyl-L-Ser + H2S
-
 Arabidopsis thaliana L-Cys + acetate
-
 ?
O-acetyl-L-Ser + H2S
-
 Aeropyrum pernix L-Cys + acetate
-
 ?
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
-
 ?
O-acetyl-L-Ser + thiosulfate
-
 Aeropyrum pernix S-sulfocysteine + sodium acetate
-
 ?
O-acetyl-L-serine
-
 Aeropyrum pernix L-cysteine + acetate
-
 ?

Subunits

Subunits Comment Organism
dimer
-
 Arabidopsis thaliana
dimer 2 * 42000, SDS-PAGE Aeropyrum pernix

Temperature Optimum [°C]

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
100
-
 pH 6.1 and 6.7, 6 h, 10% loss of activity Aeropyrum pernix

Turnover Number [1/s]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Arabidopsis thaliana
pyridoxal 5'-phosphate enzyme contains 1.2 pyridoxal phosphate per subunit Aeropyrum pernix