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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 서양
- 최종처리일시
- 20250211151339
- ISBN
- 9798382835891
- DDC
- 574
- 서명/저자
- Crystallographic and Biochemical Studies of Biosynthetic Enzymes: Using Macromolecular Structure to Understand and Engineer Terpene Biosynthesis
- 발행사항
- [Sl] : University of Pennsylvania, 2024
- 발행사항
- Ann Arbor : ProQuest Dissertations & Theses, 2024
- 형태사항
- 211 p
- 주기사항
- Source: Dissertations Abstracts International, Volume: 85-12, Section: B.
- 주기사항
- Advisor: Christianson, David W.
- 학위논문주기
- Thesis (Ph.D.)--University of Pennsylvania, 2024.
- 초록/해제
- 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.
- 일반주제명
- Biochemistry
- 일반주제명
- Chemistry
- 일반주제명
- Molecular biology
- 키워드
- Crystallography
- 키워드
- Cyclase
- 키워드
- Enzymology
- 키워드
- Terpenoids
- 기타저자
- University of Pennsylvania Chemistry
- 기본자료저록
- Dissertations Abstracts International. 85-12B.
- 전자적 위치 및 접속
- 로그인 후 원문을 볼 수 있습니다.
MARC
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■020 ▼a9798382835891
■035 ▼a(MiAaPQ)AAI31242090
■040 ▼aMiAaPQ▼cMiAaPQ
■0820 ▼a574
■1001 ▼aEaton, Samuel Anthony.
■24510▼aCrystallographic and Biochemical Studies of Biosynthetic Enzymes: Using Macromolecular Structure to Understand and Engineer Terpene Biosynthesis
■260 ▼a[Sl]▼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.
