Toward Understanding the Catalytic Mechanism of Human Paraoxonase 1: Site-Specific Mutagenesis at Position 192

Human paraoxonase 1 (h-PON1) is a serum enzyme that can hydrolyze a variety of substrates. The enzyme exhibits anti-inflammatory, anti-oxidative, anti-atherogenic, anti-diabetic, anti-microbial and organophosphate-hydrolyzing activities. Thus, h-PON1 is a strong candidate for the development of ther...

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Veröffentlicht in:	PloS one 2016-02, Vol.11 (2), p.e0147999
Hauptverfasser:	Aggarwal, Geetika, Prajapati, Rameshwar, Tripathy, Rajan K, Bajaj, Priyanka, Iyengar, A R Satvik, Sangamwar, Abhay T, Pande, Abhay H
Format:	Artikel
Sprache:	eng
Schlagworte:	Acids Amino Acid Sequence Amino acids Antiinfectives and antibacterials Aryldialkylphosphatase - chemistry Aryldialkylphosphatase - genetics Aryldialkylphosphatase - metabolism Biocatalysis Biology and Life Sciences Biotechnology Calcium - metabolism Catalysis Catalytic Domain Crystal structure Diabetes mellitus Disease E coli Enzyme Assays Enzymes Gene polymorphism Health education Humans Hydrogen Bonding Hydrolysis Inflammation Kinetics Lactones - metabolism Ligands Microorganisms Molecular dynamics Molecular Dynamics Simulation Molecular Sequence Data Molecular weight Mutagenesis Mutagenesis, Site-Directed Mutant Proteins - isolation & purification Mutants Nucleases Organophosphates - metabolism Paraoxonase Paraoxonase 1 Pharmaceutical sciences Physical Sciences Physiological aspects Poisoning Polymorphism Properties Proteins Research and Analysis Methods Sequence Alignment Simulation Structural Homology, Protein Structure Substrate specificity Substrates
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