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Literature summary extracted from

  • Renault, F.; Carus, T.; Clery-Barraud, C.; Elias, M.; Chabriere, E.; Masson, P.; Rochu, D.
    Integrative analytical approach by capillary electrophoresis and kinetics under high pressure optimized for deciphering intrinsic and extrinsic cofactors that modulate activity and stability of human paraoxonase (PON1) (2010), J. Chromatogr. B Analyt. Technol. Biomed. Life Sci., 878, 1346-1355.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.1.2 additional information binding of human phosphate binding protein amends the size of the oligomeric states and exerts a stabilizing effect on the activity Homo sapiens
3.1.1.2 phosphate
-
 synthetic construct
3.1.1.2 phosphate preserves activity with considerable fluctuations, modulates oligomeric state Homo sapiens
3.1.1.25 additional information binding of human phosphate binding protein amends the size of the oligomeric states and exerts a stabilizing effect on the activity Homo sapiens
3.1.1.25 phosphate
-
 synthetic construct
3.1.1.25 phosphate maintains activity, modulates oligomeric state Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.2 bacterially expressed chimeric G2E6 synthetic construct
3.1.1.25 bacterially expressed chimeric G2E6 synthetic construct

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.1.2 phosphate ion is bound to the catalytic calcium in the structure of crystallized recombinant G2E6 synthetic construct
3.1.1.25 phosphate ion is bound to the catalytic calcium in the structure of crystallized recombinant G2E6 synthetic construct

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.2 2-hydroxyquinoline 70% inhibition Homo sapiens
3.1.1.25 2-hydroxyquinoline
-
 Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.2 Ca2+ is essential for activity and stability of arylesterase, modulates oligomeric state Homo sapiens
3.1.1.2 Ca2+ is essential for activity and stability of arylesterase, modulates oligomeric state synthetic construct
3.1.1.25 Ca2+
-
 synthetic construct
3.1.1.25 Ca2+ is essential for activity and stability of lactonase, modulates oligomeric state Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.2 Homo sapiens
-
-
-
3.1.1.2 synthetic construct
-
 chimeric mammalian dubbed G3C9-8His, obtained using directed evolution via gene shuffling of human, rabbit, rat and mouse genes
-
3.1.1.25 Homo sapiens
-
-
-
3.1.1.25 synthetic construct
-
 chimeric mammalian dubbed G3C9-8His, obtained using directed evolution via gene shuffling of human, rabbit, rat and mouse genes
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.2 by pseudo-affinity chromatography and gel filtration Homo sapiens
3.1.1.25 by pseudo-affinity chromatography and gel filtration Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.1.2 plasma
-
 Homo sapiens
-
3.1.1.25 plasma
-
 Homo sapiens
-

Storage Stability

EC Number Storage Stability Organism
3.1.1.2 4°C, 50 mM Tris buffer, 50 mM NaCl, 1 mM CaCl2, 0.1% tergitol, pH 8.0, 1 month Homo sapiens
3.1.1.2 4°C, 50 mM Tris buffer, 50 mM NaCl, 1 mM CaCl2, 0.1% tergitol, pH 8.0, 1 month synthetic construct
3.1.1.25 4°C, 50 mM Tris buffer, 50 mM NaCl, 1 mM CaCl2, 0.1% tergitol, pH 8.0, 1 month Homo sapiens
3.1.1.25 4°C, 50 mM Tris buffer, 50 mM NaCl, 1 mM CaCl2, 0.1% tergitol, pH 8.0, 1 month synthetic construct

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.2 phenyl acetate + H2O
-
 Homo sapiens phenol + acetate
-
 ?
3.1.1.2 phenyl acetate + H2O
-
 synthetic construct phenol + acetate
-
 ?
3.1.1.25 2-coumaranone + H2O
-
 Homo sapiens (2-hydroxyphenyl)acetic acid
-
 ?
3.1.1.25 2-coumaranone + H2O
-
 synthetic construct (2-hydroxyphenyl)acetic acid
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.2 arylesterase
-
 Homo sapiens
3.1.1.2 arylesterase
-
 synthetic construct
3.1.1.25 lactonase
-
 Homo sapiens
3.1.1.25 lactonase
-
 synthetic construct

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.1.1.25 1.3
-
 2-coumaranone lactonase/human phosphate binding protein (9:1), in 50 mM Tris buffer, 1 mM NaCl, pH 8.0 at 25°C Homo sapiens
3.1.1.25 73.3
-
 2-coumaranone lactonase/human phosphate binding protein (1:1), in 50 mM Tris buffer, 1 mM NaCl, pH 8.0 at 25°C Homo sapiens
3.1.1.25 131.6
-
 2-coumaranone recombinant lactonase, in 50 mM Tris buffer, 1 mM NaCl, pH 8.0 at 25°C synthetic construct