Cloned (Comment) | Organism |
---|---|
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3) pLysS | Aeropyrum pernix |
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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Aeropyrum pernix | Q9YBL2 | - |
- |
Aeropyrum pernix DSM 11879 | Q9YBL2 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3) pLysS by nickel affinity chromatography | Aeropyrum pernix |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate | ping-pong bi-bi mechanism | Aeropyrum pernix |
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 | Comment | Organism |
---|---|---|
O-phospho-L-serine sulfhydrylase | - |
Aeropyrum pernix |
OPSS | - |
Aeropyrum pernix |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | - |
assay at | Aeropyrum pernix |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.7 | - |
assay at | Aeropyrum pernix |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | linked to lysine K127 as an internal Schiff base at the active site | Aeropyrum pernix |
General Information | Comment | Organism |
---|---|---|
additional information | Intramolecular electrostatic interaction of enzyme OPSS, overview | Aeropyrum pernix |