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Literature summary for 3.1.1.1 extracted from

  • Lange, S.; Musidlowska, A.; Schmidt-Dannert, C.; Schmitt, J.; Bornscheuer, U.T.
    Cloning, functional expression, and characterization of recombinant pig liver esterase (2001), ChemBioChem, 2, 576-582.
    View publication on PubMed
Search for more literature for 3.1.1.1

Cloned(Commentary)

Cloned (Comment) Organism
functional heterologous expression of the enzyme in Pichia pastoris was only possible after elimination of the C-terminal endoplasmic reticulum retention signal sequence His-Ala-Glu-Leu, the recombinant enzyme is secreted into the medium Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
 PLE
-
Sus scrofa PLE
-
 PLE
-

Reaction

Reaction Comment Organism Reaction ID
a carboxylic ester + H2O = an alcohol + a carboxylate active site residues are Ser203, His448, and Asp97 Sus scrofa
a

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
600
-
 recombinant enzyme Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl acetate + H2O
-
 Sus scrofa 4-nitrophenol + acetate
-
 ?
4-nitrophenyl acetate + H2O
-
 Sus scrofa PLE 4-nitrophenol + acetate
-
 ?
proline-beta-naphthylamide + H2O
-
 Sus scrofa ?
-
 ?
proline-beta-naphthylamide + H2O
-
 Sus scrofa PLE ?
-
 ?

Subunits

Subunits Comment Organism
trimer 3 * 61000-62000, SDS-PAGE Sus scrofa

Synonyms

Synonyms Comment Organism
pig liver esterase
-
 Sus scrofa
PLE
-
 Sus scrofa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
 Sus scrofa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Sus scrofa