Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.1.2 extracted from

  • Billecke, S.; Draganov, D.; Counsell, R.; Stetson, P.; Watson, C.; Hsu, C.; La Du, B.N.
    Human serum paraoxonase (PON1) isozymes Q and R hydrolyze lactones and cyclic carbonate esters (2000), Drug Metab. Dispos., 28, 1335-1342.
    View publication on PubMed
Search for more literature for 3.1.1.2

Activating Compound

Activating Compound Comment Organism Structure
dilauroyl phosphatidylcholine stimulates activity of enzyme variants Q192 and R192 Homo sapiens

Protein Variants

Protein Variants Comment Organism
C284A mutant with 44fold reduced paraoxonase activity Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
Mg2+ activity is strongly reduced when Ca2+ is removed from the purified enzyme and replaced by Zn2+ Homo sapiens
Zn2+ activity is strongly reduced when Ca2+ is removed from the purified enzyme and replaced by Zn2+ Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.27
-
 phenyl acetate enzyme variant R192 Homo sapiens
0.7
-
 phenyl acetate enzyme variant Q192 Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required for activity Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P27169 variant Q192 and R192
-

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
blood serum
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phenyl acetate + H2O enzyme protein also shows activities of EC 3.1.8.1 and EC 3.1.1.25 Homo sapiens phenol + acetate
-
 ?