EC Number   |
General Information |
Reference |
|---|
    3.1.8.1 | evolution |
enzyme SsoPox belongs to the phosphotriesterase-like lactonase (PLL) family of enzymes. SsoPox shares only about 30% sequence identity with phosphotriesterases (PTEs) but all amino acids coordinating the binuclear metal-centre are conserved. The coexistence of lactonase and phosphotriesterase activities has been already reported for many members of PLL family |
750128 |
| 3.1.8.1 | evolution |
serum paraoxonase 1 (PON1) is a native lactonase capable of promiscuously hydrolyzing a broad range of substrates, including organophosphates, esters, and carbonates. Comparison of PON1 to other organophosphatases demonstrates that either a similar gating loop or a highly buried solvent excluding active site is a common feature of these enzymes |
750914 |
| 3.1.8.1 | evolution |
Sphingobium fuliginis acquired OPH coding opd gene through lateral gene transfer |
750549 |
| 3.1.8.1 | evolution |
the enzyme is a member of phosphotriesterase-like lactonase family. The phosphotriesterase activities of phosphotriesterases (PTEs) are considered to derive from the lactonase-activities during the evolution, and phosphotriesterase-like lactonase family (PLL), is the closest protein family to PTE family based on protein-protein blast results. But members of PLL family exhibit higher lactonase activities than the phosphotriesterase activities, while the best substrates for PTEs are phosphotriesters. Enzyme mPHP is a dimer with a typical distorted (beta/alpha)8 barrel structure like other structures of PLL family and PTE family |
-, 749829 |
| 3.1.8.1 | evolution |
the phosphotriesterase activity development between PON1, EC 3.1.8.1, and DFPase, EC 3.1.8.2, is investigated by using the hybrid density functional theory method B3LYP. Structure comparisons of evolutionarily related enzymes show that the mutation of Asn270 leads to the catalytic Ca2+ ion indirectly connecting the buried structural Ca2+ ion via hydrogen bonds in DFPase. It can reduce the plasticity of enzymatic structure, and possibly change the substrate preference from paraoxon (preferred substrate of PON1) to DFP (preferred substrate of DFPase), which implies an evolutionary transition from mono- to dinuclear catalytic centers, enzyme catalysis mechanism from an evolutionary perspective, overview |
751626, 754801 |
| 3.1.8.1 | malfunction |
decrease of serum PON1 activities is usually related to many chronic diseases, such as atherosclerosis, diabetes, cancers, migraine, pulmonary tuberculosis, polycystic ovary syndrome, gastroesophageal malignancies, depression, nephritic syndrome, hemodialysis, metabolic syndrome, and liver disease. Determination of PON1 activity has a significant diagnostic value in predicting disease status |
749610 |
| 3.1.8.1 | malfunction |
insufficient organophosphate-hydrolyzing activity of native enzyme affirms the urgent need to develop improved variant(s) having enhanced organophosphate-hydrolyzing activity. Enzyme mutants show altered substrate specificity with increased activity against paraoxon and lactone substrates, overview |
749628 |
| 3.1.8.1 | malfunction |
opd null mutants of Brevundimonas diminuta fail to grow using the organophosphate insecticide methyl parathion as sole source of phosphate |
751084 |
| 3.1.8.1 | malfunction |
paraoxonase 1 knockout mice are dramatically more sensitive than wild type mice to the toxicity of chlorpyrifos oxon and diazoxon and to a lesser extent the parent phosphorothioates, chlorpyrifos and diazinon |
713690 |
| 3.1.8.1 | malfunction |
prenatal exposure to organophosphate insecticides are not associated with autism spectrum disorders and related behaviors. It is not modified by single nucleotide polymorphisms in the paraoxonase (PON1) enzyme. Analysis of the relationship of prenatal organophosphate insecticide biomarkers with reciprocal social, repetitive, and stereotypic behaviors in 8-year old children, and modification of this relationship by child PON1 polymorphisms, overview |
750427 |
