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Literature summary for 2.5.1.65 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 2.5.1.65

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Rosetta (DE3), sequencing Aeropyrum pernix

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Aeropyrum pernix
0.2
-
 Sulfide below, pH 6.7 Aeropyrum pernix
28
-
 O-acetyl-L-serine pH 6.7 Aeropyrum pernix

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Aeropyrum pernix biosynthesis of L-cysteine ?
-
 ?

Organism

Organism UniProt Comment Textmining
Aeropyrum pernix
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant OASS Aeropyrum pernix

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
50.9
-
 pH 6.7, 60°C, O-acetyl-L-serine sulfhydrylation Aeropyrum pernix

Storage Stability

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 ?
additional information biosynthesis of L-cysteine Aeropyrum pernix ?
-
 ?
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 ?
-
 ?
O-acetyl-L-serine + sulfide
-
 Aeropyrum pernix L-cysteine + acetic acid
-
 ?

Subunits

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

Synonyms

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Aeropyrum pernix
202
-
 O-acetyl-L-serine pH 6.7 Aeropyrum pernix

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.7
-
-
 Aeropyrum pernix

pH Stability

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

Cofactor

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