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Literature summary for 3.1.8.1 extracted from

  • Bajaj, P.; Tripathy, R.K.; Aggarwal, G.; Pande, A.H.
    Expression and purification of biologically active recombinant human paraoxonase 1 from inclusion bodies of Escherichia coli (2015), Protein Expr. Purif., 115, 95-101 .
    View publication on PubMed

Application

Application Comment Organism
medicine h-PON1 is a strong candidate for the development of therapeutic intervention against many diseases due to its anti-inflammatory, anti-oxidative, anti-atherogenic, anti-diabetic, anti-microbial, and organophosphate (OP)-detoxifying properties in humans Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
recombinant overexpression of the C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) in inclusion bodies Homo sapiens

Protein Variants

Protein Variants Comment Organism
H115W/R192K site-directed mutagenesis Homo sapiens
additional information development of a recombinant production method for the enzyme in Escherichia coli, which can be used for the industrial scale production of rh-PON1 enzymes. The catalytic properties of the refolded enzymes are similar to their soluble counterparts Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ dependent on Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
diethyl-paraoxon + H2O Homo sapiens
-
diethyl phosphate + 4-nitrophenol
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens P27169
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged catalytically active paraoxwild-type and mutant enzymes refolded from inclusion bodies in Escherichia coli strain BL21(DE3) by anion exchange chromatography Homo sapiens

Renatured (Commentary)

Renatured (Comment) Organism
the inactive recombinant His6-tagged wild-type and mutant enzymes present in the inclusion bodies in Escherichia coli strain BL21(DE3) are refolded to their active form using in vitro refolding, best from refolding buffer containing 200 mM TAPS, pH 8.5, 1.0 M NDSB 201, 1 mM EDTA, 2.2 mM GSH, 0.22 mM GSSH, and 10 mM CaCl2, method optimization, overview. The catalytic properties of the refolded enzymes are similar to their soluble counterparts. The extent of refolding of rh-PON1 is more when 8 M urea is used as a chaotropic agent to denature the rh-PON1 present in inclusion bodies, low concentration of rh-PON1 protein (0.005 mg/ml) is used in the refolding reaction, and when the refolding reaction is incubated for 12 h at 25°C, but low concentration of protein in in vitro refolding is generally not economical for large-scale production of protein, thus 0.020 mg/ml protein concentration is selected for the refolding reaction Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
serum
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
diethyl-paraoxon + H2O
-
Homo sapiens diethyl phosphate + 4-nitrophenol
-
?

Synonyms

Synonyms Comment Organism
h-PON1
-
Homo sapiens
human paraoxonase 1
-
Homo sapiens
paraoxonase 1
-
Homo sapiens
PON1
-
Homo sapiens

General Information

General Information Comment Organism
physiological function the serum enzyme can hydrolyze (and inactivate) a wide range of substrates. It is a multifaceted enzyme and exhibit anti-inflammatory, anti-oxidative, anti-atherogenic, anti-diabetic, anti-microbial, and organophosphate (OP)-detoxifying properties Homo sapiens