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Literature summary for 2.5.1.47 extracted from

  • Nakamura, T.; Asai, S.; Nakata, K.; Kunimoto, K.; Oguri, M.; Ishikawa, K.
    Thermostability and reactivity in organic solvent of O-phospho-L-serine sulfhydrylase from hyperthermophilic archaeon Aeropyrum pernix K1 (2015), Biosci. Biotechnol. Biochem., 79, 1280-1286.
    View publication on PubMed
Search for more literature for 2.5.1.47

Application

Application Comment Organism
synthesis enzme OASS produces novel beta-substituted L-amino acids when offered unnatural nucleophiles instead of sulfid, which is useful in producing pharmaceuticals, such as mucolytic agent L-carbocisteine and building blocks for the synthesis of pharmaceuticals and agrochemicals Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3) pLysS Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
O-acetyl-L-serine + hydrogen sulfide Escherichia coli
-
 L-cysteine + acetate
-
 ?
O-acetyl-L-serine + hydrogen sulfide Escherichia coli W3110 / ATCC 27325
-
 L-cysteine + acetate
-
 ?

Organic Solvent Stability

Organic Solvent Comment Organism
1,4-dioxane the activity of enzyme OASS-B gradually decreases as the content of organic solvent increases Escherichia coli
N,N-dimethylformamide the activity of enzyme OASS-B gradually decreases as the content of organic solvent increases Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli W3110 / ATCC 27325
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3) pLysS by nickel affinity chromatography and gel filtration Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate ping-pong bi-bi mechanism Escherichia coli
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
150
-
 pH 7.0, 37°C, 100 mM potassium phosphate Escherichia coli
667
-
 pH 7.5, 25°C, 50 mM potassium phosphate Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
O-acetyl-L-serine + hydrogen sulfide
-
 Escherichia coli L-cysteine + acetate
-
 ?
O-acetyl-L-serine + hydrogen sulfide residue Arg210 near the entrance of the active site and is important for O-acetyl-L-serine substrate recognition Escherichia coli L-cysteine + acetate
-
 ?
O-acetyl-L-serine + hydrogen sulfide
-
 Escherichia coli W3110 / ATCC 27325 L-cysteine + acetate
-
 ?
O-acetyl-L-serine + hydrogen sulfide residue Arg210 near the entrance of the active site and is important for O-acetyl-L-serine substrate recognition Escherichia coli W3110 / ATCC 27325 L-cysteine + acetate
-
 ?

Synonyms

Synonyms Comment Organism
O-acetyl-L-serine sulfhydrylase B
-
 Escherichia coli
OASS-B
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
-
 50 purified recombinant His-tagged enzyme, 1 h, completely stable at Escherichia coli
57 60 purified recombinant His-tagged enzyme, 1 h, 50% activity remaining Escherichia coli
70
-
 purified recombinant His-tagged enzyme, 1 h, inactivation Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.7
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Escherichia coli

General Information

General Information Comment Organism
additional information intramolecular electrostatic interaction of enzyme OASS-B, overview Escherichia coli