Are you looking for read ebook online? Search for your book and save it on your Kindle device, PC, phones or tablets. Download Computational And Experimental Investigation Of The Mechanism Of The Enzyme Orotidine 5 Monophosphate Decarboxylase Using Monoclonal Antibody 33f12 PDF full book. Access full book title Computational And Experimental Investigation Of The Mechanism Of The Enzyme Orotidine 5 Monophosphate Decarboxylase Using Monoclonal Antibody 33f12.
| Author | : Sogole Bahmanyar |
| Publisher | : |
| Total Pages | : 206 |
| Release | : 1998 |
| Genre | : |
| ISBN | : |
| Author | : Jeehiun K. Lee |
| Publisher | : Springer Science & Business Media |
| Total Pages | : 172 |
| Release | : 2004-06-25 |
| Genre | : Science |
| ISBN | : 9783540205661 |
K.N. Houk, D.J. Tantillo, C. Stanton, Y. Hu: What Has Theory and Crystallography Revealed About the Mechanism of Catalysis by Orotidine Monophosphate Decarboxylase?N. Wu, E.F. Pai: Crystallographic Studies of Native and Mutant Orotidine 5'Phosphate Decarboxylases; B.G.
| Author | : Heinrich Klefenz |
| Publisher | : Wiley-VCH |
| Total Pages | : 328 |
| Release | : 2002-04-22 |
| Genre | : Medical |
| ISBN | : |
This volume focuses on pharmaceutical biotechnology as a key area of life sciences. The complete range of concepts, processes and technologies of biotechnology is applied in modern industrial pharmaceutical research, development and production. The results of genome sequencing and studies of biological-genetic function are combined with chemical, micro-electronic and microsystem technology to produce medical devices and diagnostic biochips. A multitude of biologically active molecules is expanded by additional novel structures created with newly arranged gene clusters and bio-catalytic chemical processes. New organisational structures in the co-operation of institutes, companies and networks enable faster knowledge and product development and immediate application of the results of research and process development. This book is the ideal source of information for scientists and engineers in research and development, for decision-makers in biotech, pharma and chemical corporations, as well as for research institutes, but also for founders of biotech companies and people working for venture capital corporations.
| Author | : Vanessa A. Iiams |
| Publisher | : |
| Total Pages | : |
| Release | : 2011 |
| Genre | : |
| ISBN | : |
Orotidine 50́ø-monophosphate decarboxylase (OMPDC) achieves a rarely paralleled rate acceleration, yet the catalytic basis prompting this enhancement have yet to be fully elucidated. To accomplish decarboxylation, OMPDC must overcome the high energy barrier due to the localized anionic charge of the intermediate. Mechanistic studies employing enzyme mutagenesis and product or intermediate analogues were used to investigate possible transition state stabilization by a carbene resonance structure. Viability of the carbene structure depends upon a key hydrogen bond between O4 of the substrate and the amide backbone of a conserved serine or threonine. Substitution of the conserved residue with Pro resulted in a kcat/KM of 1 M-1s-1; deletion of the FUMP O4 resulted in a product analogue that does not undergo H6 exchange or inhibit decarboxylation. Hence, indirect evidence reveals the O4-backbone interaction plays an important role for binding and catalysis. OMPDC likely has honed multiple mechanisms to attain its remarkable catalysis. The successful crystallizations of OMPDC a decade ago sparked hypotheses that structure and sequence conserved residues induced productive strain on the substrate-enzyme complex. Here, we demonstrate a new source of stress: a hydrophobic pocket adjacent to the OMP carboxylate that exhibits kinetic parameters characteristic of substrate destabilization. Substitution of these residues with hydrophilic side-chains, by providing hydrogen-bonding partners, decreased kcat by 10 to 10^40́3fold. The same substitutions display very little change in the rate of product H6 exchange, supporting that this hydrophobic pocket affects the substrate-enzyme complex before the transition state. We also provide evidence that hydrophilic residues can insert water molecules into the pocket with detrimental effects to catalysis.
| Author | : Adalberto Pessoa |
| Publisher | : CRC Press |
| Total Pages | : 400 |
| Release | : 2021-07-16 |
| Genre | : Medical |
| ISBN | : 1000399842 |
Pharmaceutical Biotechnology: A Focus on Industrial Application covers the development of new biopharmaceuticals as well as the improvement of those being produced. The main purpose is to provide background and concepts related to pharmaceutical biotechnology, together with an industrial perspective. This is a comprehensive text for undergraduates, graduates and academics in biochemistry, pharmacology and biopharmaceutics, as well as professionals working on the interdisciplinary field of pharmaceutical biotechnology. Written with educators in mind, this book provides teachers with background material to enhance their classes and offers students and other readers an easy-to-read text that examines the step-by-step stages of the development of new biopharmaceuticals. Features: Discusses specific points of great current relevance in relation to new processes as well as traditional processes Addresses the main unitary operations used in the biopharmaceutical industry such as upstream and downstream Includes chapters that allow a broad evaluation of the production process Dr. Adalberto Pessoa Jr. is Full Professor at the School of Pharmaceutical Sciences of the University of São Paulo and Visiting Senior Professor at King’s College London. He has experience in enzyme and fermentation technology and in the purification processes of biotechnological products such as liquid–liquid extraction, cross-flow filtration and chromatography of interest to the pharmaceutical and food industries. Dr. Michele Vitolo is Full Professor at the School of Pharmaceutical Sciences of the University of São Paulo. He has experience in enzyme technology, in immobilization techniques (aiming the reuse of the biocatalyst) and in the operation of membrane reactors for obtaining biotechnological products of interest to the pharmaceutical, chemical and food industries. Dr. Paul F. Long is Professor of Biotechnology at King's College London and Visiting International Research Professor at the University of São Paulo. He is a microbiologist by training and his research uses a combination of bioinformatics, laboratory and field studies to discover new medicines from nature, particularly from the marine environment.
