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Literature summary extracted from

  • Yeung, D.T.; Josse, D.; Nicholson, J.D.; Khanal, A.; McAndrew, C.W.; Bahnson, B.J.; Lenz, D.E.; Cerasoli, D.M.
    Structure/function analyses of human serum paraoxonase (HuPON1) mutants designed from a DFPase-like homology model (2004), Biochim. Biophys. Acta, 1702, 67-77.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.8.1 expression of PON1 mutant enzymes in Escherichia coli Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.2 C284D no enzymic activity Homo sapiens
3.1.1.2 D269E no enzymic activity Homo sapiens
3.1.1.2 D54N no enzymic activity Homo sapiens
3.1.1.2 E313A slightly decreased activity Homo sapiens
3.1.1.2 E314A enzymic activity similar to wild-type Homo sapiens
3.1.1.2 F222D no enzymic activity Homo sapiens
3.1.1.2 F222Y increased activity with phenyl acetate, no activity with paraoxon Homo sapiens
3.1.1.2 G11A slightly enhanced activity with phenyl acetate and paraoxon Homo sapiens
3.1.1.2 G11C slightly enhanced activity with phenyl acetate and paraoxon Homo sapiens
3.1.1.2 G11S slightly enhanced activity with phenyl acetate and paraoxon Homo sapiens
3.1.1.2 H115W no enzymic activity with phenyl acetate, increased activity with paraoxon Homo sapiens
3.1.1.2 H115W/N133S no enzymic activity with phenyl acetate, slightly decreased activity with paraoxon Homo sapiens
3.1.1.2 H134W no enzymic activity Homo sapiens
3.1.1.2 H134Y no enzymic activity Homo sapiens
3.1.1.2 H285D no enzymic activity Homo sapiens
3.1.1.2 H285Y no enzymic activity Homo sapiens
3.1.1.2 L69F no enzymic activity Homo sapiens
3.1.1.2 N133S enzymic activity similar to wild-type Homo sapiens
3.1.1.2 N168E no enzymic activity Homo sapiens
3.1.1.2 N224A no enzymic activity Homo sapiens
3.1.1.2 V304A no enzymic activity Homo sapiens
3.1.8.1 C284D no enzymic activity Homo sapiens
3.1.8.1 C284D site-directed mutagenesis, inactive mutant Homo sapiens
3.1.8.1 D269E no enzymic activity Homo sapiens
3.1.8.1 D269E site-directed mutagenesis, inactive mutant Homo sapiens
3.1.8.1 D54N no enzymic activity Homo sapiens
3.1.8.1 D54N site-directed mutagenesis, inactive mutant Homo sapiens
3.1.8.1 E313A slightly decreased activity Homo sapiens
3.1.8.1 E313A site-directed mutagenesis, the mutant enzyme shows altered kinetics compared to the wild-type enzyme Homo sapiens
3.1.8.1 E314A enzymic activity similar to wild-type Homo sapiens
3.1.8.1 E314A site-directed mutagenesis, the mutant enzyme shows slightly altered kinetics compared to the wild-type enzyme Homo sapiens
3.1.8.1 F222A site-directed mutagenesis, inactive mutant Homo sapiens
3.1.8.1 F222D no enzymic activity Homo sapiens
3.1.8.1 F222D site-directed mutagenesis, inactive mutant Homo sapiens
3.1.8.1 F222Y site-directed mutagenesis, the mutant enzyme shows altered kinetics compared to the wild-type enzyme Homo sapiens
3.1.8.1 F222Y increased activity with phenyl acetate, no activity with paraoxon Homo sapiens
3.1.8.1 G11A site-directed mutagenesis, the mutant enzyme shows slightly altered kinetics compared to the wild-type enzyme Homo sapiens
3.1.8.1 G11A slightly enhanced activity with phenyl acetate and paraoxon Homo sapiens
3.1.8.1 G11C site-directed mutagenesis, the mutant enzyme shows slightly altered kinetics compared to the wild-type enzyme Homo sapiens
3.1.8.1 G11C slightly enhanced activity with phenyl acetate and paraoxon Homo sapiens
3.1.8.1 G11S site-directed mutagenesis, the mutant enzyme shows slightly altered kinetics compared to the wild-type enzyme Homo sapiens
3.1.8.1 G11S slightly enhanced activity with phenyl acetate and paraoxon Homo sapiens
3.1.8.1 H115W site-directed mutagenesis, the mutant enzyme shows reduced activity and altered kinetics compared to the wild-type enzyme Homo sapiens
3.1.8.1 H115W no enzymic activity with phenyl acetate, increased activity with paraoxon Homo sapiens
3.1.8.1 H115W/N133S site-directed mutagenesis, the mutant enzyme shows reduced activity and altered kinetics compared to the wild-type enzyme Homo sapiens
3.1.8.1 H115W/N133S no enzymic activity with phenyl acetate, slightly decreased activity with paraoxon Homo sapiens
3.1.8.1 H134W no enzymic activity Homo sapiens
3.1.8.1 H134W site-directed mutagenesis, inactive mutant Homo sapiens
3.1.8.1 H134Y no enzymic activity Homo sapiens
3.1.8.1 H134Y site-directed mutagenesis, inactive mutant Homo sapiens
3.1.8.1 H285D no enzymic activity Homo sapiens
3.1.8.1 H285D site-directed mutagenesis, inactive mutant Homo sapiens
3.1.8.1 H285Y no enzymic activity Homo sapiens
3.1.8.1 H285Y site-directed mutagenesis, inactive mutant Homo sapiens
3.1.8.1 L69F no enzymic activity Homo sapiens
3.1.8.1 L69F site-directed mutagenesis, inactive mutant Homo sapiens
3.1.8.1 N133S enzymic activity similar to wild-type Homo sapiens
3.1.8.1 N133S site-directed mutagenesis, the mutant enzyme shows slightly altered kinetics compared to the wild-type enzyme Homo sapiens
3.1.8.1 N168E no enzymic activity Homo sapiens
3.1.8.1 N168E site-directed mutagenesis, inactive mutant Homo sapiens
3.1.8.1 N224A no enzymic activity Homo sapiens
3.1.8.1 N224A site-directed mutagenesis, inactive mutant Homo sapiens
3.1.8.1 V304A no enzymic activity Homo sapiens
3.1.8.1 V304A site-directed mutagenesis, inactive mutant Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.2 0.51
-
phenyl acetate mutant E313A, pH 8.0, 25°C Homo sapiens
3.1.1.2 0.59
-
phenyl acetate mutant N133S, pH 8.0, 25°C Homo sapiens
3.1.1.2 0.61
-
phenyl acetate wild-type, pH 8.0, 25°C Homo sapiens
3.1.1.2 0.64
-
phenyl acetate mutant G11S, pH 8.0, 25°C Homo sapiens
3.1.1.2 0.67
-
phenyl acetate mutant E314A, pH 8.0, 25°C Homo sapiens
3.1.1.2 0.74
-
phenyl acetate mutant G11A or mutant G11C, pH 8.0, 25°C Homo sapiens
3.1.1.2 0.89
-
phenyl acetate mutant F222Y, pH 8.0, 25°C Homo sapiens
3.1.8.1 0.14
-
paraoxon mutant E313A, pH 10.5, 25°C Homo sapiens
3.1.8.1 0.15
-
paraoxon mutant H115W/N133S, pH 10.5, 25°C Homo sapiens
3.1.8.1 0.16
-
paraoxon wild-type, pH 10.5, 25°C Homo sapiens
3.1.8.1 0.17
-
paraoxon mutant N133S, pH 10.5, 25°C Homo sapiens
3.1.8.1 0.18
-
paraoxon mutant G11A and mutant G11S, pH 10.5, 25°C Homo sapiens
3.1.8.1 0.19
-
paraoxon mutant E314A and mutant G11C, pH 10.5, 25°C Homo sapiens
3.1.8.1 0.42
-
paraoxon mutant H115W, pH 10.5, 25°C Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.8.1 extracellular serum enzyme Homo sapiens
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.8.1 Ca2+ dependent on, Ca2+ is required for activity and is involved in the catalytic mechanism via coordinating residues Asp54, Asn168, Asn224, and Asp269, structure, overview Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.2 Homo sapiens P27169
-
-
3.1.8.1 Homo sapiens
-
-
-
3.1.8.1 Homo sapiens P27169
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.2
-
Homo sapiens
3.1.8.1
-
Homo sapiens
3.1.8.1 native PON1 from serum, overview, recombinant mutant enzymes from Escherichia coli, transient expression of mutant enzymes in HEK293 cells Homo sapiens

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.8.1 an aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol structure-function analysis, catalytic mechanism involving the residue His285, residues Leu69, His134, Phe222, and Cys284 are involved in substrate binding, Ca2+ is required for activity and is involved in the catalytic mechanism via coordinating residues Asp54, Asn168, Asn224, and Asp269 Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.1.2 blood serum
-
Homo sapiens
-
3.1.8.1 blood serum
-
Homo sapiens
-
3.1.8.1 serum
-
Homo sapiens
-

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
-
?
3.1.8.1 diethyl 4-nitrophenyl phosphate + H2O
-
Homo sapiens 4-nitrophenol + diethyl phosphate
-
?
3.1.8.1 paraoxon + H2O
-
Homo sapiens 4-nitrophenol + diethyl phosphate
-
?

Subunits

EC Number Subunits Comment Organism
3.1.8.1 More secondary structure-function analysis with enzyme structure drawn from a DFPase-like homology model, cf. EC 3.1.8.2, overview Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.1.8.1 HuPON1
-
Homo sapiens
3.1.8.1 serum paraoxonase
-
Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.2 25
-
assay at Homo sapiens
3.1.8.1 25
-
assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.2 8
-
assay at Homo sapiens
3.1.8.1 8
-
assay at Homo sapiens
3.1.8.1 10.5
-
assay at Homo sapiens