The Resource Structure, function and applications of mental-requiring enzymes : carbonic anhydrase and epi-isozizaene synthase, Julie Anne Aaron

Structure, function and applications of mental-requiring enzymes : carbonic anhydrase and epi-isozizaene synthase, Julie Anne Aaron

Label
Structure, function and applications of mental-requiring enzymes : carbonic anhydrase and epi-isozizaene synthase
Title
Structure, function and applications of mental-requiring enzymes
Title remainder
carbonic anhydrase and epi-isozizaene synthase
Statement of responsibility
Julie Anne Aaron
Creator
Contributor
Author
Degree supervisor
Subject
Genre
Language
eng
Summary
  • Cryptophane Biosensors for Targeting Human Carbonic Anhydrase. Cryptophanes represent an exciting class of xenon-encapsulating molecules that can be exploited as probes for nuclear magnetic resonance imaging. A series of carbonic anhydrase-targeting, xenon-binding cryptophane biosensors were designed and synthesized. Isothermal titration calorimery and surface plasmon resonance measurements confirmed nanomolar affinity between human carbonic anhydrase II and the cryptophane biosensors. A 1.70 Å resolution crystal structure of a cryptophane-derivatized benezenesulfonamide human carbonic anhydrase II complex was determined, and shows how an encapsulated xenon atom can be directed to a specific biological target. Furthermore, this work illustrates the utility and promise of developing xenon biosensors to diagnose human diseases characterized by the upregulation of specific carbonic anhydrase biomarkers, specifically human carbonic anhydrase IX and XII. Structural Studies of epi-Isozizaene Synthase from Streptomyces coelicolor. The X-ray crystal structure of recombinant epi -isozizaene synthase (EIZS), a sesquiterpene cyclase from Streptomyces coelicolor A3(2), has been determined at 1.60 Å resolution. Specifically, the structure of wild-type EIZS is that of its closed conformation in complex with three Mg2+ ions, inorganic pyrophosphate (PPi), and the benzyltriethylammonium cation (BTAC). Additionally, the structure of D99N EIZS has been determined in an open, ligand-free conformation at 1.90 Å resolution. Comparison of these two structures provides the first view of conformational changes required for substrate binding and catalysis in a bacterial terpenoid cyclase, and enables a comparison of substrate recognition amongst terpenoid synthases from different domains of life. Mutagenesis of aromatic residues in the enzyme active site alters the cyclization template and results in the production of alternative sesquiterpene products. The structure and activity of several active site mutants have been explored. The 1.64 Å resolution crystal structure of F198A EIZS in a complex with three Mg2+ ions, PPi, and BTAC reveals an alternative binding orientation of BTAC, whereas the crystal structures of L72V, A236G and V329A EIZS reveal an unchanged BTAC binding orientation. Alternative binding orientations of a carbocation intermediate could lead to the formation of alternative products
  • Abstract
Cataloging source
MUU
http://library.link/vocab/creatorName
Aaron, Julie Anne
Degree
Ph. D.
Dissertation note
Thesis
Dissertation year
2010.
Government publication
government publication of a state province territory dependency etc
Granting institution
University of Pennsylvania
Illustrations
illustrations
Index
no index present
LC call number
QP613.C37
LC item number
A25 2010
Literary form
non fiction
Nature of contents
  • bibliography
  • theses
http://library.link/vocab/relatedWorkOrContributorName
Christianson, David W.
http://library.link/vocab/subjectName
  • Carbonic anhydrase
  • Enzymes
  • Biosensors
  • Magnetic resonance imaging
Label
Structure, function and applications of mental-requiring enzymes : carbonic anhydrase and epi-isozizaene synthase, Julie Anne Aaron
Instantiates
Publication
Copyright
Note
  • Department of Chemistry
  • "UMI Number: 3431094."
  • "2010."
  • Thesis supervisor/advisor: David W. Christianson
Bibliography note
Includes bibliographical references (pages 158-171)
Carrier category
volume
Carrier category code
nc
Carrier MARC source
rdacarrier
Content category
text
Content type code
txt
Content type MARC source
rdacontent
Control code
938713054
Dimensions
28 cm
Extent
xvi, 171 pages
Form of item
regular print reproduction
Media category
unmediated
Media MARC source
rdamedia
Media type code
n
Other control number
UMI 3431094
Other physical details
illustrations
System control number
(OCoLC)938713054
Label
Structure, function and applications of mental-requiring enzymes : carbonic anhydrase and epi-isozizaene synthase, Julie Anne Aaron
Publication
Copyright
Note
  • Department of Chemistry
  • "UMI Number: 3431094."
  • "2010."
  • Thesis supervisor/advisor: David W. Christianson
Bibliography note
Includes bibliographical references (pages 158-171)
Carrier category
volume
Carrier category code
nc
Carrier MARC source
rdacarrier
Content category
text
Content type code
txt
Content type MARC source
rdacontent
Control code
938713054
Dimensions
28 cm
Extent
xvi, 171 pages
Form of item
regular print reproduction
Media category
unmediated
Media MARC source
rdamedia
Media type code
n
Other control number
UMI 3431094
Other physical details
illustrations
System control number
(OCoLC)938713054

Library Locations

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