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Literature summary for 3.1.1.2 extracted from

  • Harel, M.; Aharoni, A.; Gaidukov, L.; Brumshtein, B.; Khersonsky, O.; Meged, R.; Dvir, H.; Ravelli, R.B.G.; McCarthy, A.; Toker, L.; Silman, I.; Sussman, J.L.; Tawfik, D.S.
    Structure and evolution of the serum paraoxonase family of detoxifying and anti-atherosclerotic enzymes (2004), Nat. Struct. Mol. Biol., 11, 412-419.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
of mutant rePON1-G2E6 Oryctolagus cuniculus

Protein Variants

Protein Variants Comment Organism
additional information mutant rePON1-G2E6, 91% identity with wild-type and several variations deriving from human, mouse or rat wild-type enzyme, crystal structure Oryctolagus cuniculus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ included in active site Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
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recombinant enzyme diverged from wild-type with several amino acids from other enzyme genes
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Reaction

Reaction Comment Organism Reaction ID
a phenyl acetate + H2O = a phenol + acetate H115 acts as general base, H134 acts in a proton shuttle mechanismto increase H115’s basicity Oryctolagus cuniculus