ArticleProceedings of the National Academy of Sciences of the United States of America1995
Reconsideration of the catalytic center and mechanism of mammalian paraoxonase/arylesterase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 150 citations in OpenAlex.
- Review
- HDL Proteome and Alzheimer's Disease: Evidence of a Link.Antioxidants (Basel, Switzerland) · 2020Review
- Paraoxonases-1, -2 and -3: What are their functions?Chemico-biological interactions · 2016Article
- Implications of serum paraoxonase activity in obesity, diabetes mellitus, and dyslipidemia.Indian journal of endocrinology and metabolism · 2013Article
- Mechanistic Insights into the Hydrolysis of Organophosphorus Compounds by Paraoxonase-1: Exploring the Limits of Substrate Tolerance in a Promiscuous Enzyme.Journal of physical organic chemistry · 2012Article
- Hormonal and chemical regulation of paraoxonases in mice.The Journal of pharmacology and experimental therapeutics · 2012Article
- The human paraoxonase gene cluster as a target in the treatment of atherosclerosis.Antioxidants & redox signaling · 2012Review
- Paraoxonase activity and expression is modulated by therapeutics in experimental rat nonalcoholic Fatty liver disease.International journal of hepatology · 2012Article
- Relation between methylmercury exposure and plasma paraoxonase activity in inuit adults from Nunavik.Environmental health perspectives · 2011Article
- Paraoxonase 1 (PON1) polymorphisms, haplotypes and activity in predicting cad risk in North-West Indian Punjabis.PloS one · 2011Article
- In vivo administration of BL-3050: highly stable engineered PON1-HDL complexes.BMC clinical pharmacology · 2009Article
- Determination of paraoxonase 1 status without the use of toxic organophosphate substrates.Circulation. Cardiovascular genetics · 2008Article
- Pharmacogenetics of paraoxonases: a brief review.Naunyn-Schmiedeberg's archives of pharmacology · 2004Review
- Identification of paraoxonase 3 in rat liver microsomes: purification and biochemical properties.The Biochemical journal · 2003Article
- Beneficial effect of oleoylated lipids on paraoxonase 1: protection against oxidative inactivation and stabilization.The Biochemical journal · 2003Article
- Isolation and complete covalent structure of liver microsomal paraoxonase.The Biochemical journal · 1999Article
- Lactone-ring-cleaving enzyme: genetic analysis, novel RNA editing, and evolutionary implications.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Paraoxonase inhibits high-density lipoprotein oxidation and preserves its functions. A possible peroxidative role for paraoxonase.The Journal of clinical investigation · 1998Article
- DNA polymorphisms in two paraoxonase genes (PON1 and PON2) are associated with the risk of coronary heart disease.American journal of human genetics · 1998Article
- Purification and characterization of paraoxon hydrolase from rat liver.The Biochemical journal · 1997Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
For three decades, mammalian paraoxonase (A-esterase, aromatic esterase, arylesterase; PON, EC 3.1.8.1) has been thought to be a cysteine esterase demonstrating structural and mechanistic homologies with the serine esterases (cholinesterases and carboxyesterases). Human, mouse, and rabbit PONs each contain only three cysteine residues, and their positions within PON have been conserved. In purified human PON, residues Cys-41 and Cys-352 form an intramolecular disulfide bond and neither could function as an active-center cysteine. Highly purified, enzymatically active PON contains a single titratable sulfhydryl group. Thus, Cys-283 is the only probable candidate for an active-center cysteine. Through site-directed mutagenesis of the human cDNA, Cys-283 was replaced with either serine (C283S) or alanine (C283A). The expressed C283 (wild-type) enzyme was inactivated by para-hydroxymercuribenzoate, but the C283S and C283A mutant enzymes were not inactivated. C283A and C283S mutant enzymes retained both paraoxonase and arylesterase activities, and the Km values for paraoxon and phenyl acetate were similar to those of the wild type. Clearly, residue Cys-283 is free in active PON, but a free sulfhydryl group is not required for either paraoxonase or arylesterase activities. Consequently, it is necessary to examine other models for the active-site structure and catalytic mechanism of PON.
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