Abstract: Provided herein is a library of designed phosphotriesterase (PTE) enzymes, exhibiting an improved catalytic hydrolysis activity of various substrates, including nerve agents, and a general method of generating and using the same.

Abstract: Polypeptide comprising a CATH 3.40 architecture, the architecture comprising an amino acid sequence as set forth in SEQ ID NO: 18, which are capable of specifically inhibiting the activity of a 20S proteasome are disclosed. Uses thereof are also disclosed.

Abstract: The present invention relates to an organism, a tissue, a cell or an organelle expressing enzymes which allow the conversion of 2-phosphoglycolate (2-PG; also known as glycolate 2-phosphate,) into an intermediate compound of the Calvin-Benson-Bassham Cycle (CBBC) without releasing CO2. The organism, tissue, cell or organelle of the invention may be genetically engineered, transgenic and/or transplastomic so as to express at least one enzyme which is involved in this conversion. The present invention further relates to an organism, tissue, cell or organelle which comprises/expresses at least one enzyme which is involved in this conversion. The present invention further relates to a method for producing an organism, tissue, cell or organelle of the invention. The present invention further relates to a method of enzymatically converting 2-PG into an intermediate compound of the CBBC without releasing CO2.

Abstract: A genetically modified polypeptide is disclosed which comprises an amino acid sequence of phosphotriesterase (PTE) having at least twice the catalytic efficiency for a V-type nerve agent as a polypeptide which consists of the sequence as set forth in SEQ ID NO: 1, when assayed under identical conditions.

Abstract: A method for designing and selecting a protein having a stabilized structure compared to a corresponding wild type protein, and proteins having at least six amino acid substitutions with respect to a corresponding wild type protein, designed for improved thermal stability, improved specific activity and/or improved expression levels, are provided herein.

Abstract: Polypeptides are disclosed which comprise an amino acid sequence of phosphotriesterase (PTE) having enhanced catalytic efficiency for VX-type or RVX-type nerve agents. Uses thereof are also disclosed.

Abstract: A method for designing and selecting a protein having a stabilized structure compared to a corresponding wild type protein, and proteins having at least six amino acid substitutions with respect to a corresponding wild type protein, designed for improved thermal stability, improved specific activity and/or improved expression levels, are provided herein.

Abstract: A genetically modified polypeptide is disclosed which comprises an amino acid sequence of phosphotriesterase (PTE) having at least twice the catalytic efficiency for a V-type nerve agent as a polypeptide which consists of the sequence as set forth in SEQ ID NO: 1, when assayed under identical conditions.

Abstract: The present invention relates to an organism, a tissue, a cell or an organelle expressing enzymes which allow the conversion of 2-phosphoglycolate (2-PG; also known as glycolate 2-phosphate) into an intermediate compound of the Calvin-Benson-Bassham Cycle (CBBC) without releasing CO2. The organism, tissue, cell or organelle of the invention may be genetically engineered, transgenic and/or transplastomic so as to express at least one enzyme which is involved in this conversion. The present invention further relates to an organism, tissue, cell or organelle which comprises/expresses at least one enzyme which is involved in this conversion. The present invention further relates to a method for producing an organism, tissue, cell or organelle of the invention. The present invention further relates to a method of enzymatically converting 2-PG into an intermediate compound of the CBBC without releasing CO2.

Abstract: A method for designing and selecting a protein having a stabilized structure compared to a corresponding wild type protein, and proteins having at least six amino acid substitutions with respect to a corresponding wild type protein, designed for improved thermal stability, improved specific activity and/or improved expression levels, are provided herein.

Abstract: Isolated polynucleotides and polypeptides encoded therefrom are provided. These include mutated PON enzymes with increased, modified or substantially the same substrate specificity as compared to respective wild-type PON. Also provided are kits and methods using these enzymes.

Abstract: An isolated polypeptide comprising the amino acid sequence of serum paraoxonase (PON1) having catalytic efficiency of kcat/KM?106-5·107 M?1min?1 for a G-type organophosphate.

Abstract: Isolated polynucleotides and polypeptides encoded therefrom are provided. These include mutated PON enzymes with increased, modified or substantially the same substrate specificity as compared to respective wild-type PON. Also provided are kits and methods using these enzymes.

Abstract: An isolated polypeptide comprising the amino acid sequence of serum paraoxonase (PON1) having catalytic efficiency of kcat/KM?106-5·107 M?1min?1 for a G-type organophosphate.

Abstract: Isolated polynucleotides and polypeptides encoded therefrom are provided. These include mutated PON enzymes with increased, modified or substantially the same substrate specificity as compared to respective wild-type PON. Also provided are kits and methods using these enzymes.

Abstract: Isolated polynucleotides and polypeptides encoded therefrom are provided. These include mutated PON enzymes with increased, modified or substantially the same substrate specificity as compared to respective wild-type PON. Also provided are kits and methods using these enzymes.

Abstract: A method of determining an amount of total PON1 in a sample of a subject is disclosed. The method comprises: (a) contacting the sample with a compound being capable of generating at least one spectrophotometrically detectable moiety upon contact with PON1, under conditions wherein the generating is not dependent on a PON1 status; and (b) spectrophotometrically measuring a level of the moiety, thereby determining an amount of total PON1 in the sample. Kits for measuring total PON1 levels comprising the compounds are also disclosed.

Abstract: Methods and kits for diagnosing a lipid-related disorder are disclosed. Methods and pharmaceutical compositions for treating lipid-related disorders are also disclosed.

Abstract: A method of determining a level of biologically active PON enzyme is provided. The method comprising determining lactonase activity of the PON enzyme, the lactonase activity being indicative of the level of biologically active PON enzyme. Also provided are novel compounds which may be used for measuring a lactonase activity of an enzyme.

Abstract: A method for isolating the DNA encoding an enzyme is presented. The DNA is contained within a support to which the enzyme is linked, wherein the enzyme is further linked to a substrate. When the enzyme reacts with the substrate, the product remains linked to the enzyme. The product linked to the enzyme which is linked to the support containing the DNA encoding the enzyme is isolated, thereby isolating the DNA encoding the enzyme. In this manner an expression library of enzymes produced by mutagenesis can be screened for mutated active enzyme, and thereby obtain the mutated DNA encoding the mutated active enzyme.