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Crystallographic and Biochemical Studies of Biosynthetic Enzymes: Using Macromolecular Structure to Understand and Engineer Terpene Biosynthesis.
Crystallographic and Biochemical Studies of Biosynthetic Enzymes: Using Macromolecular Str...
Contents Info
Crystallographic and Biochemical Studies of Biosynthetic Enzymes: Using Macromolecular Structure to Understand and Engineer Terpene Biosynthesis.
Material Type  
 학위논문
 
0017161322
Date and Time of Latest Transaction  
20250211151339
ISBN  
9798382835891
DDC  
574
Author  
Eaton, Samuel Anthony.
Title/Author  
Crystallographic and Biochemical Studies of Biosynthetic Enzymes: Using Macromolecular Structure to Understand and Engineer Terpene Biosynthesis.
Publish Info  
[S.l.] : University of Pennsylvania., 2024
Publish Info  
Ann Arbor : ProQuest Dissertations & Theses, 2024
Material Info  
211 p.
General Note  
Source: Dissertations Abstracts International, Volume: 85-12, Section: B.
General Note  
Advisor: Christianson, David W.
학위논문주기  
Thesis (Ph.D.)--University of Pennsylvania, 2024.
Abstracts/Etc  
요약Terpenoid natural products comprise the largest and most structurally diverse class of natural products observed to date. These complex secondary metabolites are synthesized in all domains of life, exhibit potent bioactivities, and are critically important compounds in a number of chemical industries, including the pharmaceutical, energy, and cosmetic industries. Despite the remarkable diversity observed among this class of natural products, all terpenes derive from a mere handful of common primary metabolites, collectively known as isoprenoid diphosphates. Specialized enzymes of secondary metabolism (e.g.; terpenoid cyclases or aromatic prenyltransferases) use these common substrates to generate the diverse hydrocarbon scaffolds that underlie over 102,000 terpenoid natural products. Crystallographic and biochemical studies which illuminate the structure-function relationships of these enzymes help to unravel the complex molecular basis of catalysis. Understanding the structures and chemical mechanisms of biosynthetic enzymes is a crucial step in guiding structure-based engineering approaches to generate new and useful synthetic biology tools. This thesis examines the structural and chemical biology of two microbial terpenoid biosynthetic enzymes, epi-Isozizaene Synthase and Reverse N-Dimethylallyl-L-Tryptophan Synthase 1.
Subject Added Entry-Topical Term  
Biochemistry.
Subject Added Entry-Topical Term  
Chemistry.
Subject Added Entry-Topical Term  
Molecular biology.
Index Term-Uncontrolled  
Crystallography
Index Term-Uncontrolled  
Cyclase
Index Term-Uncontrolled  
Enzymology
Index Term-Uncontrolled  
Prenyltransferases
Index Term-Uncontrolled  
Terpenoids
Added Entry-Corporate Name  
University of Pennsylvania Chemistry
Host Item Entry  
Dissertations Abstracts International. 85-12B.
Electronic Location and Access  
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Control Number  
joongbu:658670
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