The Experts below are selected from a list of 2046789 Experts worldwide ranked by ideXlab platform

Magdalena Korczynska - One of the best experts on this subject based on the ideXlab platform.

  • Functional Annotation and Structural Characterization of a Novel Lactonase Hydrolyzing d‑Xylono-1,4-lactone-5-phosphate and l‑Arabino-1,4-lactone-5-phosphate
    2015
    Co-Authors: Magdalena Korczynska, Dao Feng Xiang, Zhening Zhang, Tamari Narindoshvili, Siddhesh S Kamat, Howard J Williams, Peter Kolb, Shawn S. Chang, B Hillerich
    Abstract:

    A novel lactonase from Mycoplasma synoviae 53 (MS53_0025) and Mycoplasma agalactiae PG2 (MAG_6390) was characterized by protein structure determination, molecular docking, gene Context Analysis, and library screening. The crystal structure of MS53_0025 was determined to a resolution of 2.06 Å. This protein adopts a typical amidohydrolase (β/α)8-fold and contains a binuclear zinc center located at the C-terminal end of the β-barrel. A phosphate molecule was bound in the active site and hydrogen bonds to Lys217, Lys244, Tyr245, Arg275, and Tyr278. Both docking and gene Context Analysis were used to narrow the theoretical substrate profile of the enzyme, thus directing empirical screening to identify that MS53_0025 and MAG_6390 catalyze the hydrolysis of d-xylono-1,4-lactone-5-phosphate (2) with kcat/Km values of 4.7 × 104 and 5.7 × 104 M–1 s–1 and l-arabino-1,4-lactone-5-phosphate (7) with kcat/Km values of 1.3 × 104 and 2.2 × 104 M–1 s–1, respectively. The identification of the substrate profile of these two phospho-furanose lactonases emerged only when all methods were integrated and therefore provides a blueprint for future substrate identification of highly related amidohydrolase superfamily members

  • functional annotation and structural characterization of a novel lactonase hydrolyzing d xylono 1 4 lactone 5 phosphate and l arabino 1 4 lactone 5 phosphate
    Biochemistry, 2014
    Co-Authors: Magdalena Korczynska, Dao Feng Xiang, Zhening Zhang, Tamari Narindoshvili, Siddhesh S Kamat, Howard J Williams, Shawn Chang, Peter Kolb, B Hillerich
    Abstract:

    A novel lactonase from Mycoplasma synoviae 53 (MS53_0025) and Mycoplasma agalactiae PG2 (MAG_6390) was characterized by protein structure determination, molecular docking, gene Context Analysis, and library screening. The crystal structure of MS53_0025 was determined to a resolution of 2.06 A. This protein adopts a typical amidohydrolase (β/α)8-fold and contains a binuclear zinc center located at the C-terminal end of the β-barrel. A phosphate molecule was bound in the active site and hydrogen bonds to Lys217, Lys244, Tyr245, Arg275, and Tyr278. Both docking and gene Context Analysis were used to narrow the theoretical substrate profile of the enzyme, thus directing empirical screening to identify that MS53_0025 and MAG_6390 catalyze the hydrolysis of d-xylono-1,4-lactone-5-phosphate (2) with kcat/Km values of 4.7 × 104 and 5.7 × 104 M–1 s–1 and l-arabino-1,4-lactone-5-phosphate (7) with kcat/Km values of 1.3 × 104 and 2.2 × 104 M–1 s–1, respectively. The identification of the substrate profile of these t...

B Hillerich - One of the best experts on this subject based on the ideXlab platform.

  • Functional Annotation and Structural Characterization of a Novel Lactonase Hydrolyzing d‑Xylono-1,4-lactone-5-phosphate and l‑Arabino-1,4-lactone-5-phosphate
    2015
    Co-Authors: Magdalena Korczynska, Dao Feng Xiang, Zhening Zhang, Tamari Narindoshvili, Siddhesh S Kamat, Howard J Williams, Peter Kolb, Shawn S. Chang, B Hillerich
    Abstract:

    A novel lactonase from Mycoplasma synoviae 53 (MS53_0025) and Mycoplasma agalactiae PG2 (MAG_6390) was characterized by protein structure determination, molecular docking, gene Context Analysis, and library screening. The crystal structure of MS53_0025 was determined to a resolution of 2.06 Å. This protein adopts a typical amidohydrolase (β/α)8-fold and contains a binuclear zinc center located at the C-terminal end of the β-barrel. A phosphate molecule was bound in the active site and hydrogen bonds to Lys217, Lys244, Tyr245, Arg275, and Tyr278. Both docking and gene Context Analysis were used to narrow the theoretical substrate profile of the enzyme, thus directing empirical screening to identify that MS53_0025 and MAG_6390 catalyze the hydrolysis of d-xylono-1,4-lactone-5-phosphate (2) with kcat/Km values of 4.7 × 104 and 5.7 × 104 M–1 s–1 and l-arabino-1,4-lactone-5-phosphate (7) with kcat/Km values of 1.3 × 104 and 2.2 × 104 M–1 s–1, respectively. The identification of the substrate profile of these two phospho-furanose lactonases emerged only when all methods were integrated and therefore provides a blueprint for future substrate identification of highly related amidohydrolase superfamily members

  • functional annotation and structural characterization of a novel lactonase hydrolyzing d xylono 1 4 lactone 5 phosphate and l arabino 1 4 lactone 5 phosphate
    Biochemistry, 2014
    Co-Authors: Magdalena Korczynska, Dao Feng Xiang, Zhening Zhang, Tamari Narindoshvili, Siddhesh S Kamat, Howard J Williams, Shawn Chang, Peter Kolb, B Hillerich
    Abstract:

    A novel lactonase from Mycoplasma synoviae 53 (MS53_0025) and Mycoplasma agalactiae PG2 (MAG_6390) was characterized by protein structure determination, molecular docking, gene Context Analysis, and library screening. The crystal structure of MS53_0025 was determined to a resolution of 2.06 A. This protein adopts a typical amidohydrolase (β/α)8-fold and contains a binuclear zinc center located at the C-terminal end of the β-barrel. A phosphate molecule was bound in the active site and hydrogen bonds to Lys217, Lys244, Tyr245, Arg275, and Tyr278. Both docking and gene Context Analysis were used to narrow the theoretical substrate profile of the enzyme, thus directing empirical screening to identify that MS53_0025 and MAG_6390 catalyze the hydrolysis of d-xylono-1,4-lactone-5-phosphate (2) with kcat/Km values of 4.7 × 104 and 5.7 × 104 M–1 s–1 and l-arabino-1,4-lactone-5-phosphate (7) with kcat/Km values of 1.3 × 104 and 2.2 × 104 M–1 s–1, respectively. The identification of the substrate profile of these t...

Siddhesh S Kamat - One of the best experts on this subject based on the ideXlab platform.

  • Functional Annotation and Structural Characterization of a Novel Lactonase Hydrolyzing d‑Xylono-1,4-lactone-5-phosphate and l‑Arabino-1,4-lactone-5-phosphate
    2015
    Co-Authors: Magdalena Korczynska, Dao Feng Xiang, Zhening Zhang, Tamari Narindoshvili, Siddhesh S Kamat, Howard J Williams, Peter Kolb, Shawn S. Chang, B Hillerich
    Abstract:

    A novel lactonase from Mycoplasma synoviae 53 (MS53_0025) and Mycoplasma agalactiae PG2 (MAG_6390) was characterized by protein structure determination, molecular docking, gene Context Analysis, and library screening. The crystal structure of MS53_0025 was determined to a resolution of 2.06 Å. This protein adopts a typical amidohydrolase (β/α)8-fold and contains a binuclear zinc center located at the C-terminal end of the β-barrel. A phosphate molecule was bound in the active site and hydrogen bonds to Lys217, Lys244, Tyr245, Arg275, and Tyr278. Both docking and gene Context Analysis were used to narrow the theoretical substrate profile of the enzyme, thus directing empirical screening to identify that MS53_0025 and MAG_6390 catalyze the hydrolysis of d-xylono-1,4-lactone-5-phosphate (2) with kcat/Km values of 4.7 × 104 and 5.7 × 104 M–1 s–1 and l-arabino-1,4-lactone-5-phosphate (7) with kcat/Km values of 1.3 × 104 and 2.2 × 104 M–1 s–1, respectively. The identification of the substrate profile of these two phospho-furanose lactonases emerged only when all methods were integrated and therefore provides a blueprint for future substrate identification of highly related amidohydrolase superfamily members

  • functional annotation and structural characterization of a novel lactonase hydrolyzing d xylono 1 4 lactone 5 phosphate and l arabino 1 4 lactone 5 phosphate
    Biochemistry, 2014
    Co-Authors: Magdalena Korczynska, Dao Feng Xiang, Zhening Zhang, Tamari Narindoshvili, Siddhesh S Kamat, Howard J Williams, Shawn Chang, Peter Kolb, B Hillerich
    Abstract:

    A novel lactonase from Mycoplasma synoviae 53 (MS53_0025) and Mycoplasma agalactiae PG2 (MAG_6390) was characterized by protein structure determination, molecular docking, gene Context Analysis, and library screening. The crystal structure of MS53_0025 was determined to a resolution of 2.06 A. This protein adopts a typical amidohydrolase (β/α)8-fold and contains a binuclear zinc center located at the C-terminal end of the β-barrel. A phosphate molecule was bound in the active site and hydrogen bonds to Lys217, Lys244, Tyr245, Arg275, and Tyr278. Both docking and gene Context Analysis were used to narrow the theoretical substrate profile of the enzyme, thus directing empirical screening to identify that MS53_0025 and MAG_6390 catalyze the hydrolysis of d-xylono-1,4-lactone-5-phosphate (2) with kcat/Km values of 4.7 × 104 and 5.7 × 104 M–1 s–1 and l-arabino-1,4-lactone-5-phosphate (7) with kcat/Km values of 1.3 × 104 and 2.2 × 104 M–1 s–1, respectively. The identification of the substrate profile of these t...

Dao Feng Xiang - One of the best experts on this subject based on the ideXlab platform.

  • Functional Annotation and Structural Characterization of a Novel Lactonase Hydrolyzing d‑Xylono-1,4-lactone-5-phosphate and l‑Arabino-1,4-lactone-5-phosphate
    2015
    Co-Authors: Magdalena Korczynska, Dao Feng Xiang, Zhening Zhang, Tamari Narindoshvili, Siddhesh S Kamat, Howard J Williams, Peter Kolb, Shawn S. Chang, B Hillerich
    Abstract:

    A novel lactonase from Mycoplasma synoviae 53 (MS53_0025) and Mycoplasma agalactiae PG2 (MAG_6390) was characterized by protein structure determination, molecular docking, gene Context Analysis, and library screening. The crystal structure of MS53_0025 was determined to a resolution of 2.06 Å. This protein adopts a typical amidohydrolase (β/α)8-fold and contains a binuclear zinc center located at the C-terminal end of the β-barrel. A phosphate molecule was bound in the active site and hydrogen bonds to Lys217, Lys244, Tyr245, Arg275, and Tyr278. Both docking and gene Context Analysis were used to narrow the theoretical substrate profile of the enzyme, thus directing empirical screening to identify that MS53_0025 and MAG_6390 catalyze the hydrolysis of d-xylono-1,4-lactone-5-phosphate (2) with kcat/Km values of 4.7 × 104 and 5.7 × 104 M–1 s–1 and l-arabino-1,4-lactone-5-phosphate (7) with kcat/Km values of 1.3 × 104 and 2.2 × 104 M–1 s–1, respectively. The identification of the substrate profile of these two phospho-furanose lactonases emerged only when all methods were integrated and therefore provides a blueprint for future substrate identification of highly related amidohydrolase superfamily members

  • functional annotation and structural characterization of a novel lactonase hydrolyzing d xylono 1 4 lactone 5 phosphate and l arabino 1 4 lactone 5 phosphate
    Biochemistry, 2014
    Co-Authors: Magdalena Korczynska, Dao Feng Xiang, Zhening Zhang, Tamari Narindoshvili, Siddhesh S Kamat, Howard J Williams, Shawn Chang, Peter Kolb, B Hillerich
    Abstract:

    A novel lactonase from Mycoplasma synoviae 53 (MS53_0025) and Mycoplasma agalactiae PG2 (MAG_6390) was characterized by protein structure determination, molecular docking, gene Context Analysis, and library screening. The crystal structure of MS53_0025 was determined to a resolution of 2.06 A. This protein adopts a typical amidohydrolase (β/α)8-fold and contains a binuclear zinc center located at the C-terminal end of the β-barrel. A phosphate molecule was bound in the active site and hydrogen bonds to Lys217, Lys244, Tyr245, Arg275, and Tyr278. Both docking and gene Context Analysis were used to narrow the theoretical substrate profile of the enzyme, thus directing empirical screening to identify that MS53_0025 and MAG_6390 catalyze the hydrolysis of d-xylono-1,4-lactone-5-phosphate (2) with kcat/Km values of 4.7 × 104 and 5.7 × 104 M–1 s–1 and l-arabino-1,4-lactone-5-phosphate (7) with kcat/Km values of 1.3 × 104 and 2.2 × 104 M–1 s–1, respectively. The identification of the substrate profile of these t...

Zhening Zhang - One of the best experts on this subject based on the ideXlab platform.

  • Functional Annotation and Structural Characterization of a Novel Lactonase Hydrolyzing d‑Xylono-1,4-lactone-5-phosphate and l‑Arabino-1,4-lactone-5-phosphate
    2015
    Co-Authors: Magdalena Korczynska, Dao Feng Xiang, Zhening Zhang, Tamari Narindoshvili, Siddhesh S Kamat, Howard J Williams, Peter Kolb, Shawn S. Chang, B Hillerich
    Abstract:

    A novel lactonase from Mycoplasma synoviae 53 (MS53_0025) and Mycoplasma agalactiae PG2 (MAG_6390) was characterized by protein structure determination, molecular docking, gene Context Analysis, and library screening. The crystal structure of MS53_0025 was determined to a resolution of 2.06 Å. This protein adopts a typical amidohydrolase (β/α)8-fold and contains a binuclear zinc center located at the C-terminal end of the β-barrel. A phosphate molecule was bound in the active site and hydrogen bonds to Lys217, Lys244, Tyr245, Arg275, and Tyr278. Both docking and gene Context Analysis were used to narrow the theoretical substrate profile of the enzyme, thus directing empirical screening to identify that MS53_0025 and MAG_6390 catalyze the hydrolysis of d-xylono-1,4-lactone-5-phosphate (2) with kcat/Km values of 4.7 × 104 and 5.7 × 104 M–1 s–1 and l-arabino-1,4-lactone-5-phosphate (7) with kcat/Km values of 1.3 × 104 and 2.2 × 104 M–1 s–1, respectively. The identification of the substrate profile of these two phospho-furanose lactonases emerged only when all methods were integrated and therefore provides a blueprint for future substrate identification of highly related amidohydrolase superfamily members

  • functional annotation and structural characterization of a novel lactonase hydrolyzing d xylono 1 4 lactone 5 phosphate and l arabino 1 4 lactone 5 phosphate
    Biochemistry, 2014
    Co-Authors: Magdalena Korczynska, Dao Feng Xiang, Zhening Zhang, Tamari Narindoshvili, Siddhesh S Kamat, Howard J Williams, Shawn Chang, Peter Kolb, B Hillerich
    Abstract:

    A novel lactonase from Mycoplasma synoviae 53 (MS53_0025) and Mycoplasma agalactiae PG2 (MAG_6390) was characterized by protein structure determination, molecular docking, gene Context Analysis, and library screening. The crystal structure of MS53_0025 was determined to a resolution of 2.06 A. This protein adopts a typical amidohydrolase (β/α)8-fold and contains a binuclear zinc center located at the C-terminal end of the β-barrel. A phosphate molecule was bound in the active site and hydrogen bonds to Lys217, Lys244, Tyr245, Arg275, and Tyr278. Both docking and gene Context Analysis were used to narrow the theoretical substrate profile of the enzyme, thus directing empirical screening to identify that MS53_0025 and MAG_6390 catalyze the hydrolysis of d-xylono-1,4-lactone-5-phosphate (2) with kcat/Km values of 4.7 × 104 and 5.7 × 104 M–1 s–1 and l-arabino-1,4-lactone-5-phosphate (7) with kcat/Km values of 1.3 × 104 and 2.2 × 104 M–1 s–1, respectively. The identification of the substrate profile of these t...