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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 Structure to Understand and Engineer Terpene Biosynthesis.
상세정보
- 자료유형
- 학위논문
- Control Number
- 0017161322
- International Standard Book Number
- 9798382835891
- Dewey Decimal Classification Number
- 574
- Main Entry-Personal Name
- Eaton, Samuel Anthony.
- Publication, Distribution, etc. (Imprint
- [S.l.] : University of Pennsylvania., 2024
- Publication, Distribution, etc. (Imprint
- Ann Arbor : ProQuest Dissertations & Theses, 2024
- Physical Description
- 211 p.
- General Note
- Source: Dissertations Abstracts International, Volume: 85-12, Section: B.
- General Note
- Advisor: Christianson, David W.
- Dissertation Note
- Thesis (Ph.D.)--University of Pennsylvania, 2024.
- Summary, 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
- 로그인을 한후 보실 수 있는 자료입니다.
- Control Number
- joongbu:658670
MARC
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■1001 ▼aEaton, Samuel Anthony.
■24510▼aCrystallographic and Biochemical Studies of Biosynthetic Enzymes: Using Macromolecular Structure to Understand and Engineer Terpene Biosynthesis.
■260 ▼a[S.l.]▼bUniversity of Pennsylvania. ▼c2024
■260 1▼aAnn Arbor▼bProQuest Dissertations & Theses▼c2024
■300 ▼a211 p.
■500 ▼aSource: Dissertations Abstracts International, Volume: 85-12, Section: B.
■500 ▼aAdvisor: Christianson, David W.
■5021 ▼aThesis (Ph.D.)--University of Pennsylvania, 2024.
■520 ▼aTerpenoid 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.
■590 ▼aSchool code: 0175.
■650 4▼aBiochemistry.
■650 4▼aChemistry.
■650 4▼aMolecular biology.
■653 ▼aCrystallography
■653 ▼aCyclase
■653 ▼aEnzymology
■653 ▼aPrenyltransferases
■653 ▼aTerpenoids
■690 ▼a0487
■690 ▼a0485
■690 ▼a0307
■71020▼aUniversity of Pennsylvania▼bChemistry.
■7730 ▼tDissertations Abstracts International▼g85-12B.
■790 ▼a0175
■791 ▼aPh.D.
■792 ▼a2024
■793 ▼aEnglish
■85640▼uhttp://www.riss.kr/pdu/ddodLink.do?id=T17161322▼nKERIS▼z이 자료의 원문은 한국교육학술정보원에서 제공합니다.
