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Ram Sasisekharan. Wrick, Michael A Massachusetts Institute of Technology. Dept. of Mechanical Engineering. Massachusetts Institute of Technology. Department of Mechanical Engineering 2008-03-27T18:24:43Z 2008-03-27T18:24:43Z 2006 2007 http://hdl.handle.net/1721.1/40931 212409215 Thesis (S.B.)--Massachusetts Institute of Technology, Dept. of Mechanical Engineering, June 2007. Includes bibliographical references (leaves 19-21). In recent studies related to injury to the central nervous system, researchers have found that galactosaminoglycans can serve as inhibitors to neuron regeneration. The chondroitinase enzyme family is comprised of several bacterial lyases known to dissolve galactosaminoglycans in the extracellular matrix. Although several studies have shown the benefit of using chondroitinase enzymes for treatment, there is much to learn about its enzyme-substrate complex. For the purpose of this research, we focus on the processing of two key galactosaminoglycan substrates, chondroitin-6-sulfate and dermatan sulfate. Through a systematic approach, we investigate the active site of chondroitinase ABC I with biological and structural studies. We demonstrate that calcium, a divalent ion, potentially increases the activity of chondroitinase ABC I when processing dermatan sulfate. From this we gain insight into the structural make-up of the chondroitinase ABC I enzyme, allowing us to optimize our approach for targeting inhibitory substrates that prevent regeneration in the central nervous system. by Michael A. Wrick. S.B. 22 leaves eng Massachusetts Institute of Technology M.I.T. theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. See provided URL for inquiries about permission. http://dspace.mit.edu/handle/1721.1/7582 Mechanical Engineering. Understanding the catalytic machinery of chondroitinase ABC I in processing dermatan sulfate Thesis application/pdf false Publication unknown unknown <Publication xmlns="https://www.openaire.eu/cerif-profile/1.1/" id="7da9c81a-20a9-4b8b-9628-a00379cffda9"> <Type xmlns="https://www.openaire.eu/cerif-profile/vocab/COAR_Publication_Types">http://purl.org/coar/resource_type/c_1843</Type> <Language>eng</Language> <Title>Understanding the catalytic machinery of chondroitinase ABC I in processing dermatan sulfate</Title> <PublishedIn> <Publication> </Publication> </PublishedIn> <PublicationDate>2007</PublicationDate> <Authors> <Author> <DisplayName>Wrick, Michael A</DisplayName> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> </Authors> <Editors> </Editors> <Publishers> <Publisher> <DisplayName>Massachusetts Institute of Technology</DisplayName> <OrgUnit /> </Publisher> </Publishers> <License>http://dspace.mit.edu/handle/1721.1/7582</License> <Keyword>Mechanical Engineering.</Keyword> <Abstract>In recent studies related to injury to the central nervous system, researchers have found that galactosaminoglycans can serve as inhibitors to neuron regeneration. The chondroitinase enzyme family is comprised of several bacterial lyases known to dissolve galactosaminoglycans in the extracellular matrix. Although several studies have shown the benefit of using chondroitinase enzymes for treatment, there is much to learn about its enzyme-substrate complex. For the purpose of this research, we focus on the processing of two key galactosaminoglycan substrates, chondroitin-6-sulfate and dermatan sulfate. Through a systematic approach, we investigate the active site of chondroitinase ABC I with biological and structural studies. We demonstrate that calcium, a divalent ion, potentially increases the activity of chondroitinase ABC I when processing dermatan sulfate. From this we gain insight into the structural make-up of the chondroitinase ABC I enzyme, allowing us to optimize our approach for targeting inhibitory substrates that prevent regeneration in the central nervous system.</Abstract> <Access xmlns="http://purl.org/coar/access_right" > </Access> </Publication>