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Literature summary for extracted from

  • Oda, Y.; Mino, K.; Ishikawa, K.; Ataka, M.
    Three-dimensional structure of a new enzyme, O-phosphoserine sulfhydrylase, involved in l-cysteine biosynthesis by a hyperthermophilic archaeon, Aeropyrum pernix K1, at 2.0 A resolution (2005), J. Mol. Biol., 351, 334-344.
    View publication on PubMed


Cloned (Comment) Organism
expression of wild-type, selenomethinonine-labeled, and mutant R297A enzymes in Escherichia coli Aeropyrum pernix

Crystallization (Commentary)

Crystallization (Comment) Organism
wild-type and selennomethionine-labeled enzyme, sitting drop method, 20 mg/ml protein in solution with 0.1 mM pyridoxal 5'-phosphate, 3 mM 2-mercaptoethanol, reservoir solution contains 0.1 M sodium cacodylate, pH 7.0, 0.2 M sodium acetate, 21% w/v poylethylene glycol 8000, and 3 mM 2-mercaptoethanol, mixture of equal volumes of protein and reservoir solution of 0.0035 ml, equilibration against 0.1 ml reservoir solution, 25°C, 2 weeks, crystallization of the selenomethinone enzyme at pH 6.0, multi-wave anomalous dispersion, X-ray diffraction structure determination and analysis at 2.0 A resolution Aeropyrum pernix

Protein Variants

Protein Variants Comment Organism
R297A site-directed mutagenesis, highly reduced activity with phospho-L-serine compared to the wild-type enzyme 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 enzyme is involved in L-cysteine biosynthesis L-cysteine + phosphate


Organism UniProt Comment Textmining
Aeropyrum pernix

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type, selenomethinonine-labeled, and mutant R297A enzymes from Escherichia coli Aeropyrum pernix


Reaction Comment Organism Reaction ID
O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate active site structure, modeling of substrate binding at the active site with Arg297 being crucial for activity Aeropyrum pernix

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
mutant R297A, substrate O-phospho-L-serine Aeropyrum pernix
mutant R297A, substrate O-acetyl-L-serine Aeropyrum pernix
wild-type enzyme, substrate O-acetyl-L-serine Aeropyrum pernix
wild-type enzyme, substrate O-phospho-L-serine Aeropyrum pernix

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme also shows low L-cystathionine forming activity Aeropyrum pernix ?
O-acetyl-L-serine + hydrogen sulfide
Aeropyrum pernix L-cysteine + acetate
O-phospho-L-serine + hydrogen sulfide
Aeropyrum pernix L-cysteine + phosphate
O-phospho-L-serine + hydrogen sulfide enzyme is involved in L-cysteine biosynthesis Aeropyrum pernix L-cysteine + phosphate


Subunits Comment Organism
More an enzyme monomer consists of 3 domains, structure overview Aeropyrum pernix


Synonyms Comment Organism
Aeropyrum pernix

Temperature Optimum [°C]

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


Cofactor Comment Organism Structure
pyridoxal 5'-phosphate binding site in the cleft between middle and C-terminal domains through a covalent link to Lys127 Aeropyrum pernix