Pattraranee Limphong (5 results)
- Softcover
Seller: Mispah books, Redhill, SURRE, United KingdomMispah books
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paperback. Condition: New. NEW. SHIPS FROM MULTIPLE LOCATIONS. book.
Language: English
Published by LAP LAMBERT Academic Publishing Dez 2011, 2011
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Seller: BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, GermanyBuchWeltWeit Ludwig Meier e.K.
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Taschenbuch. Condition: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -The glyoxalase system is made up of two enzymes that detoxify methylglyoxal and the other reactive oxoaldehydes, which are produced as a normal part of metabolism. In this book, the characterization of two GLX2-like isozymes from Ar…abidopsis thaliana and human GLX2 is presented. Our work demonstrates that GLX2-1 is not a glyoxalase 2; however, the protein does contain a dinuclear metal center. We found that GLX2-1 does catalyze the hydrolysis of beta-lactam antibiotics. Overall results suggest that different isozymes of GLX2 have different metal centers and different activities. Also, both the highly conserved metal binding domain (T-H-X-H-X-D-H) and the substrate binding ligands need to be concerned to be considered when classifying glyoxalase 2 enzymes. The results in this book further our understanding of the GLX2 enzymes. It has helped elucidate the structure, function, and mechanism of these enzymes. Our results are contributing to the ultimate goal in glyoxalase research in search of inhibitors that can be used as potential drugs in the treatment of glyoxalase system-related diseases, and the results also suggest that this enzyme may be the template for evolving new functions 152 pp. Englisch.
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Seller: moluna, Greven, Germanymoluna
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Condition: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Autor/Autorin: Limphong PattraraneeDr. Pattraranee Limphong obtained her Ph.D degree in Biochemistry from Miami University, Ohio in 2009. She has worked as a post-doctoral research associate in the Division of Cardiol…ogy, University of Utah School .
Language: English
Published by LAP LAMBERT Academic Publishing Dez 2011, 2011
- Softcover
- Print on Demand
Seller: buchversandmimpf2000, Emtmannsberg, BAYE, Germanybuchversandmimpf2000
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Taschenbuch. Condition: Neu. This item is printed on demand - Print on Demand Titel. Neuware -The glyoxalase system is made up of two enzymes that detoxify methylglyoxal and the other reactive oxoaldehydes, which are produced as a normal part of metabolism. In this book, the characterization of two GLX2-like isozymes from Arabid…opsis thaliana and human GLX2 is presented. Our work demonstrates that GLX2-1 is not a glyoxalase 2; however, the protein does contain a dinuclear metal center. We found that GLX2-1 does catalyze the hydrolysis of beta-lactam antibiotics. Overall results suggest that different isozymes of GLX2 have different metal centers and different activities. Also, both the highly conserved metal binding domain (T-H-X-H-X-D-H) and the substrate binding ligands need to be concerned to be considered when classifying glyoxalase 2 enzymes. The results in this book further our understanding of the GLX2 enzymes. It has helped elucidate the structure, function, and mechanism of these enzymes. Our results are contributing to the ultimate goal in glyoxalase research in search of inhibitors that can be used as potential drugs in the treatment of glyoxalase system-related diseases, and the results also suggest that this enzyme may be the template for evolving new functionsVDM Verlag, Dudweiler Landstraße 99, 66123 Saarbrücken 152 pp. Englisch.
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Seller: AHA-BUCH GmbH, Einbeck, GermanyAHA-BUCH GmbH
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Taschenbuch. Condition: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - The glyoxalase system is made up of two enzymes that detoxify methylglyoxal and the other reactive oxoaldehydes, which are produced as a normal part of metabolism. In this book, the characterization of two GLX2-like isozymes from Arabido…psis thaliana and human GLX2 is presented. Our work demonstrates that GLX2-1 is not a glyoxalase 2; however, the protein does contain a dinuclear metal center. We found that GLX2-1 does catalyze the hydrolysis of beta-lactam antibiotics. Overall results suggest that different isozymes of GLX2 have different metal centers and different activities. Also, both the highly conserved metal binding domain (T-H-X-H-X-D-H) and the substrate binding ligands need to be concerned to be considered when classifying glyoxalase 2 enzymes. The results in this book further our understanding of the GLX2 enzymes. It has helped elucidate the structure, function, and mechanism of these enzymes. Our results are contributing to the ultimate goal in glyoxalase research in search of inhibitors that can be used as potential drugs in the treatment of glyoxalase system-related diseases, and the results also suggest that this enzyme may be the template for evolving new functions.
