Over-Expression and Characterization of a Glyoxalase 2 Like Enzyme : Spectroscopic and Kinetic Studies of metalloenzyme

Pattraranee Limphong

ISBN 10: 3847319590 / ISBN 13: 9783847319597

Published by LAP LAMBERT Academic Publishing, 2011

About this Item

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 Arabidopsis 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.

Seller Inventory # 9783847319597

Bibliographic Details

• Title: Over-Expression and Characterization of a Glyoxalase 2 Like Enzyme : Spectroscopic and Kinetic Studies of metalloenzyme
• Publisher: LAP LAMBERT Academic Publishing
• Publication Date: 2011
• Language: English
• ISBN 10: 3847319590
• ISBN 13: 9783847319597
• Binding: Taschenbuch
• Condition: Neu
• Dimensions: 220W x 150H x 10D millimeters 220 millimeters width by 150 millimeters height by 10 millimeters depth
• Weight: 244 grams

About this title

Synopsis

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 Arabidopsis 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

About the Author

Dr. 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 Cardiology, University of Utah School of Medicine since 2009. Dr. Limphong is the author and co-author of several articles published in Biochemistry journals.