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Literature summary for 2.5.1.65 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

Cloned(Commentary)

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
O-phospho-L-serine + hydrogen sulfide Aeropyrum pernix
-
L-cysteine + phosphate
-
?
O-phospho-L-serine + hydrogen sulfide Aeropyrum pernix DSM 11879
-
L-cysteine + phosphate
-
?

Organic Solvent Stability

Organic Solvent Comment Organism
1,4-dioxane the activity of enzyme OPSS increases in the reaction mixture containing the organic solvent, such as N,N-dimethylformamide and 1,4-dioxane Aeropyrum pernix
N,N-dimethylformamide the activity of enzyme OPSS increases in the reaction mixture containing the organic solvent, such as N,N-dimethylformamide and 1,4-dioxane Aeropyrum pernix

Organism

Organism UniProt Comment Textmining
Aeropyrum pernix Q9YBL2
-
-
Aeropyrum pernix DSM 11879 Q9YBL2
-
-

Purification (Commentary)

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

Reaction

Reaction Comment Organism Reaction ID
O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate ping-pong bi-bi mechanism Aeropyrum pernix

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information OPSS is able to catalyze the synthetic reactions of various unnatural amino acids from OPS and nucleophiles that can substitute for sulfide Aeropyrum pernix ?
-
?
additional information OPSS is able to catalyze the synthetic reactions of various unnatural amino acids from OPS and nucleophiles that can substitute for sulfide Aeropyrum pernix DSM 11879 ?
-
?
O-phospho-L-serine + hydrogen sulfide
-
Aeropyrum pernix L-cysteine + phosphate
-
?
O-phospho-L-serine + hydrogen sulfide residue Arg297 near the entrance of the active site and is important for O-phospho-L-serine substrate recognition Aeropyrum pernix L-cysteine + phosphate
-
?
O-phospho-L-serine + hydrogen sulfide
-
Aeropyrum pernix DSM 11879 L-cysteine + phosphate
-
?
O-phospho-L-serine + hydrogen sulfide residue Arg297 near the entrance of the active site and is important for O-phospho-L-serine substrate recognition Aeropyrum pernix DSM 11879 L-cysteine + phosphate
-
?

Synonyms

Synonyms Comment Organism
O-phospho-L-serine sulfhydrylase
-
Aeropyrum pernix
OPSS
-
Aeropyrum pernix

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
80
-
assay at Aeropyrum pernix

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
-
100 purified recombinant His-tagged enzyme, 1 h, completely stable at Aeropyrum pernix

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate linked to lysine K127 as an internal Schiff base at the active site Aeropyrum pernix

General Information

General Information Comment Organism
additional information Intramolecular electrostatic interaction of enzyme OPSS, overview Aeropyrum pernix