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Literature summary for 3.1.1.2 extracted from

  • Rochu, D.; Renault, F.; Clery-Barraud, C.; Chabriere, E.; Masson, P.
    Stability of highly purified human paraoxonase (PON1): Association with human phosphate binding protein (HPBP) is essential for preserving its active conformation(s) (2007), Biochim. Biophys. Acta, 1774, 874-883.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Homo sapiens P27169
-
-

Source Tissue

Source Tissue Comment Organism Textmining
blood plasma
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phenyl acetate + H2O
-
Homo sapiens phenol + acetate
-
?

Subunits

Subunits Comment Organism
oligomer once purified, human PON1 is as a mixture of at least two oligomerization states. The absence of human phosphate binding protein favors homo-oligomerization of PON1 into different state(s) of higher molecular size Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Homo sapiens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
human PON1 exhibits intrinsically a remarkable thermal stability. The association of human phosphate binding protein, though it does not change the denaturation temperature, strongly contributes to slow the rate of irreversible denaturation Homo sapiens
60
-
complete loss of activity above Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Homo sapiens